Journal articles: 'Cashin'

1

IVERSON, STEPHANIE DAY. ""Early" Bonnie Cashin, before Bonnie Cashin Designs, Inc." Studies in the Decorative Arts 8, no. 1 (October 2000): 108–24. http://dx.doi.org/10.1086/studdecoarts.8.1.40662762.

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Kim, Injoo, Seung A. Lee, and George F. Sarofeen. "Characteristics of Signature Bonnie Cashin Designs." International Journal of Costume and Fashion 15, no. 1 (June 30, 2015): 51–74. http://dx.doi.org/10.7233/ijcf.2015.15.1.051.

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Kim, Injoo, and Juhyung Woo. "A Study on the Design of Bonnie Cashin." Korean Society of Fashion Design 18, no. 2 (June 30, 2018): 125–43. http://dx.doi.org/10.18652/2018.18.2.8.

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4

Bates, Timothy. "Rejoinder to Sheryll Cashin: Programs as Token Gestures." Economic Development Quarterly 14, no. 3 (August 2000): 250–55. http://dx.doi.org/10.1177/089124240001400303.

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Dallari, Sueli Gandolfi. "Resenha internacional: Universal Health Coverage for inclusive and sustainable development: a synthesis of 11 country case studies." Revista de Direito Sanitário 15, no. 3 (April 14, 2015): 325. http://dx.doi.org/10.11606/issn.2316-9044.v15i3p325-329.

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Resenha sobre a publicação "Universal Health Coverage for inclusive and sustainable development: a synthesis of 11 country case studies", Akiko Maeda, Edson Araujo, Cheryl Cashin, Joseph Harris, Naoki Ikegami, and Michael R. Reich (org.), International Bank for Reconstruction and Development / The World Bank <http://dx.doi.org/10.1596/978-1-4648-0297-3>

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6

Wang, Cathy. "Place, not race: A new vision of opportunity in America, by Sheryll Cashin." Journal of Urban Affairs 39, no. 4 (May 2, 2017): 586–88. http://dx.doi.org/10.1111/juaf.12271.

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7

Cohen, Joanna. "War Matters: Material Culture in the Civil War Era ed. by Joan E. Cashin." Journal of the Civil War Era 9, no. 4 (2019): 650–52. http://dx.doi.org/10.1353/cwe.2019.0084.

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8

Woods, Michael E. "War Matters: Material Culture in the Civil War Era ed. by Joan E. Cashin." Register of the Kentucky Historical Society 117, no. 2 (2019): 400–402. http://dx.doi.org/10.1353/khs.2019.0040.

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9

Sears, Christine E. "War Matters: Material Culture in the Civil War Era ed. by Joan E. Cashin." Journal of Southern History 85, no. 4 (2019): 914–16. http://dx.doi.org/10.1353/soh.2019.0254.

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10

Omelicheva, Mariya Y., and Olga Avdeyeva. "Teaching with Lecture or Debate? Testing the Effectiveness of Traditional versus Active Learning Methods of Instruction." PS: Political Science & Politics 41, no. 03 (June 18, 2008): 603–7. http://dx.doi.org/10.1017/s1049096508080815.

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Lecture is, arguably, the oldest known instructional technique used in the university setting. Since it was first employed in Plato's Academy, lecture has become an indispensable part of teaching favored across the college and university curriculum. Recently, this time-honored method of instruction has come under attack for its presumed inability to foster higher order cognitive and attitudinal goals (Cashin 1985; Day 1980; Frederick 1999; Renner 1993). Critics of traditional lecture-based formats call for their replacement with active learning approaches that provide students with an opportunity to meaningfully talk, interact, write, read, and reflect on the content, ideas, and issues of an academic subject (Meyers and Jones 1993, 6).

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11

Bech, Anne-Marie, and K. Rotvig Kristiansen. "Milk protein polymorphism in Danish dairy cattle and the influence of genetic variants on milk yield." Journal of Dairy Research 57, no. 1 (February 1990): 53–62. http://dx.doi.org/10.1017/s0022029900026601.

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SummaryIn milk samples from 549 cows of the breeds Danish Jersey, Red Danish Dairy Cattle (RDM), and Black and White Danish Dairy Cattle (SDM) the genetic polymorphisms of the αs1, β and K-cascin and β-lactoglobulin (β-Lg) loci were determined by isoelectric focusing in agarose gels. The results of the screening were comparcd with results obtained by Larsen & Thymann (1966). In addition, the genetic linkage of the three casein loci was studied, and the association between milk protein genotypes and yields in first and second lactations of milk, fat and protein were investigated.The distribution of genotypes of all four milk protein Systems was different from breed to breed.For Jersey cows, significant differences in the gene frequencies from the results of the 1966 investigation were found for αs1 and K-casein and β-Lg. For SDM cows a change in the K-casein frequency had occurred whereas for RDM cows no changes were found.Linkage between some of the casein loci was found within ail three breeds. For the RDM breed the possible linkage between αs1-casein and the other caseins could not be tested bccause nearly ail thc cows were homozygous for the αs1-cascin-B genotypes.β-Casein genotypes were associated with yield parameters in ail breeds. The A2A2 genotype of this protein gave higher yields of milk, fat, and protein in the second lactation than thc A1A1 genotype.

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12

Chown, Nick. "Modified hermeneutic phenomenological approach toward individuals who have autism: A response to newman, cashin and waters." Research in Nursing & Health 34, no. 6 (September 6, 2011): 435–36. http://dx.doi.org/10.1002/nur.20459.

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13

Sugarbaker, Paul H., and Kurt Van der Speeten. "Cashin and Graf: long-term intraperitoneal 5-fluorouracil is superior to adjuvant FOLFOX in a randomized trial." Journal of Gastrointestinal Oncology 12, S1 (April 2021): S136. http://dx.doi.org/10.21037/jgo-2020-16.

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14

Phillips, Jason. "War Stuff: The Struggle for Human and Environmental Resources in the American Civil War by Joan E. Cashin." Journal of the Civil War Era 9, no. 4 (2019): 647–50. http://dx.doi.org/10.1353/cwe.2019.0083.

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15

Swanson, Drew. "War Stuff: The Struggle for Human and Environmental Resources in the American Civil War by Joan E. Cashin." Journal of Southern History 86, no. 1 (2020): 170–73. http://dx.doi.org/10.1353/soh.2020.0018.

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16

Mauldin, Erin Stewart. "War Stuff: The Struggle for Human and Environmental Resources in the American Civil War by Joan E. Cashin." Civil War History 65, no. 4 (2019): 411–13. http://dx.doi.org/10.1353/cwh.2019.0051.

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17

Nelson, Megan Kate. "War Stuff: The Struggle for Human and Environmental Resources in the American Civil War. By Joan E. Cashin." Environmental History 24, no. 2 (January 28, 2019): 389–91. http://dx.doi.org/10.1093/envhis/emy152.

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18

Chanat, E., P. Martin, and M. Ollivier-Bousquet. "Alpha(S1)-casein is required for the efficient transport of beta- and kappa-casein from the endoplasmic reticulum to the Golgi apparatus of mammary epithelial cells." Journal of Cell Science 112, no. 19 (October 1, 1999): 3399–412. http://dx.doi.org/10.1242/jcs.112.19.3399.

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In lactating mammary epithelial cells, interaction between caseins is believed to occur after their transport out of the endoplasmic reticulum. We show here that, in alpha(S1)-casein-deficient goats, the rate of transport of the other caseins to the Golgi apparatus is highly reduced whereas secretion of whey proteins is not significantly affected. This leads to accumulation of immature caseins in distended rough endoplasmic reticulum cisternae. Casein micelles, nevertheless, were still observed in secretory vesicles. In contrast, no accumulation was found in mammary epithelial cells which lack beta-casein. In mammary epithelial cells secreting an intermediate amount of alpha(S1)-casein, less casein accumulated in the rough endoplasmic reticulum, and the transport of alpha(S1)-casein to the Golgi occurred with kinetics similar to that of control cells. In prolactin-treated mouse mammary epithelial HC11 cells, which do not express alpha(S)-caseins, endoplasmic reticulum accumulation of beta-casein was also observed. The amount of several endoplasmic reticulum-resident proteins increased in conjunction with casein accumulation. Finally, the permeabilization of rough endoplasmic reticulum vesicles allowed the recovery of the accumulated caseins in soluble form. We conclude that optimal export of the caseins out of the endoplasmic reticulum is dependent upon alpha(S1)-casein. Our data suggest that alpha(S1)-casein interacts with the other caseins in the rough endoplasmic reticulum and that the formation of this complex is required for their efficient export to the Golgi.

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19

Rao, M. Govinda, and Kunal Sen. "Internal Migration, Center-State Grants, and Economic Growth in the States of India: A Comment on Cashin and Sahay." Staff Papers - International Monetary Fund 44, no. 2 (June 1997): 283. http://dx.doi.org/10.2307/3867545.

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20

Li-Chan, Eunice, and Shuryo Nakai. "Enzymic dephosphorylation of bovine casein to improve acid clotting properties and digestibility for infant formula." Journal of Dairy Research 56, no. 3 (May 1989): 381–90. http://dx.doi.org/10.1017/s0022029900028843.

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SummaryTo improve acid clotting properties, enzymic dephosphorylation of caseins with calf intestinal alkaline phosphatase (CAP) or potato acid phosphatase (PAP) was investigated. Greater dephosphorylation was achieved using αs1- or β-casein as substrates, compared to whole casein or skim milk. Electrophoresis of PAP-modified caseins revealed bands with lower mobility and a multibanded pattern in the β-casein region which was similar to that of human β-casein. On the other hand, CAP modification produced electrophoretic bands having lower mobility of the β-casein component, but with higher mobility in the αs1-casein component as well as increased net negative charge in the CAP-casein. PAP-casein formed a fine dispersion upon acidification to pH 4. with a microstructure similar to that of acidified human casein. Greater initial rates of hydrolysis by pepsin at pH 4 were observed for both CAP- and PAP-modified caseins, compared to bovine and human caseins. The rate and extent of hydrolysis remained high for CAP-casein but tended to level off with PAP-casein during sequential digestion with pepsin and pancreatin. There may be advantages in the use of partial dephosphorylation to improve acid clotting and digestibility properties of bovine casein for infant feeding.

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21

Partschefeld, C., J. Schreiner, U. Schwarzenbolz, and T. Henle. "Studies on Enzymatic Crosslinking of Casein Micelles." Czech Journal of Food Sciences 27, Special Issue 1 (June 24, 2009): S99—S101. http://dx.doi.org/10.17221/938-cjfs.

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The aim of our study was to gain insights into the reactions occurring in casein micelles during enzymatic modification with microbial transglutaminase (mTG). Therefore, UHT-treated milk was incubated with varying amounts of mTG and the caseins were analysed using different analytical methods. Regarding the casein species, it was observed that β -casein was crosslinked to a higher extent than the α-caseins. From this it can be suggested that β-casein is mainly located in the outer space of the micellar structure and therefore better accessible to mTG than α-caseins, which are located predominantly in the interior. Furthermore, it was demonstrated by gel-permeation chromatography and RP-HPLC that the caseins are fixed within the micellar structure, by what the ratio of extramicellar casein decreased. We conclude that an isopeptide network in the outer β -casein rich “shell” of the micelle is formed by mTG, which is responsible for the increased micellar stability.

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22

Goldfield, David. "Reviews of Books:Paternalism in a Southern City: Race, Religion, and Gender in Augusta, Georgia Edward J. Cashin, Glenn T. Eskew." American Historical Review 107, no. 2 (April 2002): 553–54. http://dx.doi.org/10.1086/532360.

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23

Southern, Kyle. "Place, Not Race: A New Vision of Opportunity in America by Sheryll Cashin. Boston: Beacon Press, 2014. 176 pp., $25.95." American Journal of Education 122, no. 1 (November 2015): 166–69. http://dx.doi.org/10.1086/683290.

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24

Holt, Carl, D. Thomas Davies, and Andrew J. R. Law. "Effects of colloidal calcium phosphate content and free calcium ion concentration in the milk serum on the dissociation of bovine casein micelles." Journal of Dairy Research 53, no. 4 (November 1986): 557–72. http://dx.doi.org/10.1017/s0022029900033082.

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SummaryThe strength of binding of the individual caseins and the nature of the bonding within bovine casein micelles were examined through dissociation of the micelles by dialysis of skim milk either against phosphate-free buffers containing 3 or 6 mm-CaCl2, or against buffers that were nearly saturated with respect to micellar calcium phosphate, but which had a free Ca2+ concentration in the range 0·4–5·9 mm. Dissociation was followed by ultracentrifuging the dialysed milks and determining the partition of the total and the individual caseins between the pellet and serum. During dialysis against the phosphate-free buffers both colloidal Ca and Pi in the milks decreased and about 30 % of the Pi could be removed without significant casein dissociation. With further loss of Pi, however, increasing dissociation occurred and the proportions of the individual caseins retained in the casein pellet were in the order αs2- > αs1- > β- ≈ κ-casein. Dialysis against the calcium phosphate buffers resulted in no loss of colloidal Pi but colloidal Ca increased with the free Ca2+ concentration of the buffer. Little change in the casein partition occurred in the presence of more than 1 mm free Ca2+, but serum casein increased markedly at lower levels, and the strength of binding of the individual caseins in the pelleted casein was in the order αs2-> αs1- > β- > κ-casein. In both types of buffer, dissociation is considered to occur through the breaking of linkages between the caseins and inorganic constituents. Analysis of the amino acids in a calcium phosphate-rich material obtained after exhaustive proteolytic digestion of casein micelles suggests that these linkages involve the phosphate centres of the caseins.

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25

Davies, D. Thomas, and Andrew J. R. Law. "Quantitative fractionation of casein mixtures by fast protein liquid chromatography." Journal of Dairy Research 54, no. 3 (August 1987): 369–76. http://dx.doi.org/10.1017/s0022029900025541.

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SummaryAlkylation of whole casein samples by reaction with cysteamine and cystamine in a bis-tris-propane–urea buffer (pH 7·0) followed by fast protein liquid chromatography (FPLC) at 20°C on a Mono Q HR5/5 column in the same buffer and using a NaCl gradient led to good resolution of the whole casein into fractions representing (i) γ2- plus γ3-caseins, (ii) κ-caseins, (iii) β-casein, (iv) αs2-caseins and (v) αsl-caseins, together with small amounts of unidentified materials. Quantitatively the FPLC values agreed well with those for αs1-, β-, αs2- and γ2- plus γ3-caseins obtained by ion-exchange chromatography on DEAE cellulose, Whatman DE52 and with those for º-caseins obtained by gel-permeation chromatography on Sephadex G–150.

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26

Singh, Harjinder, Albert Flynn, and Patrick F. Fox. "Binding of zinc to bovine and human milk proteins." Journal of Dairy Research 56, no. 2 (May 1989): 235–48. http://dx.doi.org/10.1017/s0022029900026455.

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SummaryZn binding by whole bovine and human casein and by purified bovine caseins and whey proteins was investigated by equilibrium dialysis. Bovine αs1 casein had the greatest Zn-binding capacity (˜ 11 atoms Zn/mol). Protein aggregation was observed as Zn concentration was increased and- the protein precipitated at a free Zn concentration of 1·7 mM. Zn binding increased with increasing pH in the range 5·4–7·0 and decreased with increasing ionic strength. Competition between Zn and Ca was observed for binding to αs1-casein indicating common binding sites for these two metals. Bovine β-casein bound up to 8 atoms Zn/ mol and precipitated at a free Zn concentration of ˜ 2·5 mM, while K-casein bound 1–2 atoms Zn/mol. Whole bovine and human casein bound 5–8 atoms Zn/mol and precipitated at a free Zn concentration of ˜ 2·0 mM. Scatchard plots for Zn binding to caseins showed upward convexity, possibly due to Zn-induced association of caseins. Apparent average association constants (K¯app) for all caseins were similar (log K¯app 3·0–3·2). Enzymic dephosphorylation of αs1- or whole bovine casein markedly reduced, but did not eliminate, Zn binding. Thus, phosphoserine residues appeared to be the primary Zn-binding sites in caseins. With the exception of bovine serum albumin. which bound over 8 atoms Zn/mol, the bovine whey proteins, β-lactoglobulin, α-lactalbumin and lactotransferrin, had little capacity for Zn binding.

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27

Lefèvre, Christophe M., Julie A. Sharp, and Kevin R. Nicholas. "Characterisation of monotreme caseins reveals lineage-specific expansion of an ancestral casein locus in mammals." Reproduction, Fertility and Development 21, no. 8 (2009): 1015. http://dx.doi.org/10.1071/rd09083.

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Using a milk-cell cDNA sequencing approach we characterised milk-protein sequences from two monotreme species, platypus (Ornithorhynchus anatinus) and echidna (Tachyglossus aculeatus) and found a full set of caseins and casein variants. The genomic organisation of the platypus casein locus is compared with other mammalian genomes, including the marsupial opossum and several eutherians. Physical linkage of casein genes has been seen in the casein loci of all mammalian genomes examined and we confirm that this is also observed in platypus. However, we show that a recent duplication of β-casein occurred in the monotreme lineage, as opposed to more ancient duplications of α-casein in the eutherian lineage, while marsupials possess only single copies of α- and β-caseins. Despite this variability, the close proximity of the main α- and β-casein genes in an inverted tail–tail orientation and the relative orientation of the more distant kappa-casein genes are similar in all mammalian genome sequences so far available. Overall, the conservation of the genomic organisation of the caseins indicates the early, pre-monotreme development of the fundamental role of caseins during lactation. In contrast, the lineage-specific gene duplications that have occurred within the casein locus of monotremes and eutherians but not marsupials, which may have lost part of the ancestral casein locus, emphasises the independent selection on milk provision strategies to the young, most likely linked to different developmental strategies. The monotremes therefore provide insight into the ancestral drivers for lactation and how these have adapted in different lineages.

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28

Vítková, M., P. Rauch, and L. Fukal. "Optimisation of indirect competitive ELISAs of a-, b-, and k-caseins for the recognition of thermal and proteolytic treatment of milk and milk products." Czech Journal of Food Sciences 20, No. 2 (November 18, 2011): 53–62. http://dx.doi.org/10.17221/3510-cjfs.

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Polyclonal antibodies were raised against six immunogens (three native and three thermally treated casein fractions: a+b-casein, k-casein and whole casein). Using these antibodies the procedures of an indirect competitive enzyme immunoassay (ELISA) were constructed, optimised and characterised for determination of each immunogen. It was found that ELISA of caseins is very specific without any interferences of whey proteins and with proportionally low cross-interactions between caseins. Detection limits for a-, b-, and k-caseins and whole casein were 110, 49, 58 and 505 ng/ml, respectively. The coefficient of variation was lower than 12% in intra-assay and lower than 9% in inter-assay. The developed ELISA format was used to study changes in casein immunoreactivity during heat-treatment and proteolytic hydrolysis. Heating below 100°C did not change the milk immunoreactivity but heating above 100°C caused its significant changes. Depending on type of proteolytic treatment (with enzyme preparation Pancreatin or with microbial cultures of Lactobacillus helveticus and Lactococcus) a decrease and an increase in casein immunoreactivity were observed. While Pancreatin reduced the casein immunoreactivity substantially (5–1000 times in dependence on the casein type), the more gentle proteolysis by bacteria caused not only its reduction (even 100 times at k-casein) but also its increase (1.5 times at a-casein).  

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29

Johnson, Matthew J. "Sheryll Cashin, Loving: Interracial Intimacy in America and the Threat to White Supremacy. Boston: Beacon Press, 2017. Pp. 237. $26.95 (cloth)." Journal of African American History 106, no. 2 (March 1, 2021): 356–58. http://dx.doi.org/10.1086/713329.

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30

Dalgleish, Douglas G., and Andrew J. R. Law. "pH-Induced dissociation of bovine casein micelles. I. Analysis of liberated caseins." Journal of Dairy Research 55, no. 4 (November 1988): 529–38. http://dx.doi.org/10.1017/s0022029900033306.

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SummaryThe dissociation of caseins of different types from casein micelles in milk, acidified to different pH values in the range 4·9–6·7, and at temperatures of 4, 20 and 30 °C, has been studied. In contrast to a number of previous findings, it was shown that caseins of all types were dissociated from the micelles, although in all cases β-casein was in highest concentration. The amounts and proportions of all of the caseins were found to be pH- and temperature-dependent, especially the former. Studies of the proportions of the different caseins liberated suggested that, at a defined temperature, the proportions of κ;- and αs2-caseins were independent of pH, while the proportions of β- and αsl-caseins were variable, changes in one being compensated by changes in the other. The manner in which the proportions of the αsl-casein and β-caseins changes with pH was found to be temperature-dependent.

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31

Ono, Tomotada, Hideaki Kohno, Satoshi Odagiri, and Toshio Takagi. "Subunit components of casein micelles from bovine, ovine, caprine and equine milks." Journal of Dairy Research 56, no. 1 (February 1989): 61–68. http://dx.doi.org/10.1017/s0022029900026224.

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SummarySubunit components of ovine, caprine and equine casein micelles were separated by gel chromatography using a TSK-G4000SW high-performance column and the subunit components of the fractions analysed and compared with bovine casein. Molecular weights of the casein complexes were determined by the combined use of high-performance gel chromatography and low-angle laser light scattering. The caprine and ovine caseins were separated into three peaks (F2, F3 and F4) which were similar to those of bovine casein with respect to composition and molecular weight (500, 100 and 23 K). These F2, F3 and F4 peaks consisted mainly of αs- and κ-casein, αs- and β-casein and β-casein respectively. The equine casein was separated into two components corresponding to F3 and F4 of bovine casein. These F3 and F4 peaks consisted mainly of αs- and β-casein and β-casein respectively. The molecular weight of equine F3 (850 K) was different from that of the other three species. The contents of F2 and F4 in these caseins were dependent on the contents of κ-casein and β-casein respectively.

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Coolbear, Kate P., David F. Elgar, Tim Coolbear, and John S. Ayers. "Comparative study of methods for the isolation and purification of bovine κ-casein and its hydrolysis by chymosin." Journal of Dairy Research 63, no. 1 (February 1996): 61–71. http://dx.doi.org/10.1017/s002202990003154x.

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Summaryκ-Casein was purified from a single batch of whole acid casein (κ-A variant) using different methods in order to compare their merits in producing a purified material with a carbohydrate and phosphate heterogeneity representative of the whole κ-casein complement in milk. Ion-exchange methods of purification gave products of higher purity than precipitation techniques involving final purification by ethanol fractionation, but all methods resulted in κ-caseins of apparently similar heterogeneity and chemical composition. The purified κ-caseins were hydrolysed with chymosin and the derived macropeptides isolated. These were all virtually identical as determined by reversed-phase chromatography and gel electrophoresis. Some observations on chymosin hydrolysis of κ-casein were made. In addition to formation of the major para-κ-casein (Glu1–Phe105) and macropeptide (Met106–Val169), chymosin hydrolysis at pH 6·6 also resulted in two minor para-κ-caseins with N-termini corresponding to Phe18 and Ser33 of κ-casein. At pH 5·5 and 4·5 para-κ-casein was rapidly hydrolysed into at least six fragments, one of which had an N-terminus corresponding to Trp76 of κ-casein. At pH 6·6, 5·5 and 4·5 the κ-casein macropeptide was stable to chymosin, but at pH 2·3 it was hydrolysed by chymosin into fragments with N-termini corresponding to Met106, He125, Ala138, Val139, Thr145 and Glu147 of κ-casein.

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Wilson, Michael, Daniel M. Mulvihill, William J. Donnelly, and Brian P. Gill. "Surface active properties at the air–water interface of β-casein and its fragments derived by plasmin proteolysis." Journal of Dairy Research 56, no. 3 (May 1989): 487–94. http://dx.doi.org/10.1017/s0022029900028971.

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Summaryβ-Casein, was enzymically modified by incubation with plasmin to yield γ-caseins and proteose peptones. Whole γ-, γ1-, γ2/γ3-caseins and whole proteose peptone (pp) were isolated from the hydrolysate mixture. The time dependence of surface tension at the air-water interface of solutions of β-casein and its plasmin derived fragments, at concentrations of 10−1 to 10−4% (w/v) protein, pH 7.0, was determined, at 25 °C, using a drop volume apparatus. The ranking of the proteins with respect to rate of reduction of surface tension, during the first rate determining step, at 10-2% (w/v) protein, was γ2/γ3 ≫ pp > whole γ- > γ1- > β-casein. The ranking of the proteins with respect to surface pressures attained after 40 min (π40) was concentration dependent. γ2/γ3-Caseins were found to be very surface active, decreasing surface tension rapidly and giving a high π40. γ1 Casein decreased surface activity somewhat faster than β-casein, but generally reached a lower π40. Whole γ-casein reflected the properties of both γ1 and γ2/γ3-caseins. Proteose peptone was found to decrease surface tension rapidly during the initial rate determining step; it gave a relatively high π40 at a bulk phase concentration of 10−3% (w/v) protein, but, it was the least surface active protein at 10−1 and 10−2% (w/v) protein.

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34

Brown, Joanna R., Andrew J. R. Law, and Christopher H. Knight. "Changes in casein composition of goats' milk during the course of lactation: physiological inferences and technological implications." Journal of Dairy Research 62, no. 3 (August 1995): 431–39. http://dx.doi.org/10.1017/s0022029900031137.

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SummaryFive British Saanen goats were milk sampled during the first 39 weeks of lactation to determine changes in casein composition. Caseins were separated by anion- and cation-exchange FPLC to determine the relative amounts of the individual caseins. Acid, alkaline and SDS-PAGE were used to determine possible genetic polymorphisms and observe any lactational changes. Total casein nitrogen was determined using a micro-Kjeldahl method and this allowed the concentrations of individual caseins to be calculated. The milk of one animal, which had the deduced genotype αs1-CnAB, showed higher concentrations of both total and αs1-casein. The remainder of the group were either heterozygous αs1-CnBE or, more probably, homozygous αs1-CnE and produced milk of a generally lower protein concentration. Both FPLC and PAGE results showed that the relative amounts and concentrations of αs2-casein decreased with stage of lactation, consistent with its susceptibility to proteolysis. The relative amounts of the breakdown products of plasmin attack on β-casein, γ-caseins, were highly negatively correlated with milk yield (r = –0·942, P < 0·001) in the declining phase of lactation, reflecting the gradual involution of the gland at this time. The relative amount of κ-casein increased by ∼ 50% after peak lactation and its concentration almost doubled near the end of lactation. These compositional changes may alter the processing qualities of goats' milk in relation to cheese production.

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35

Green, M. R. "Identification of human milk kappa-casein on polyacrylamide gels by differential staining with Ethyl-Stains-all and chymosin sensitivity." Journal of Histochemistry & Cytochemistry 34, no. 2 (February 1986): 147–50. http://dx.doi.org/10.1177/34.2.2418097.

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Ethyl-Stains-all (ESA), a cationic carbocyanine dye that stains phosphorylated, sialylated, and unmodified proteins differentially, was used to stain a human casein fraction enriched for its kappa-casein-like characteristics. The staining properties and chymosin sensitivity of this fraction were compared with those of human milk and bovine casein proteins. Phosphorylated human and bovine beta caseins stained blue with ESA. The sialic acid-containing bovine kappa-casein stained blue-green. The human kappa-like fraction was enriched for a protein that stained blue-green with ESA. Both bovine kappa-casein and the human blue-green-staining protein were susceptible to chymosin digestion at lower concentrations of chymosin than that required for digestion of beta-caseins. In each case, following chymosin digestion, a green-staining peptide of lower molecular weight replaced the original protein and para-kappa-casein was formed. Identification of human kappa-casein on SDS-polyacrylamide gels was based on its differential staining with ESA and chymosin sensitivity with respect to beta-casein.

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Chianese, Lina, Rosalba Mauriello, Luigi Moio, Nunziatina Intorcia, and Francesco Addeo. "Determination of ovine casein heterogeneity using gel electrophoresis and immunochemical techniques." Journal of Dairy Research 59, no. 1 (February 1992): 39–47. http://dx.doi.org/10.1017/s0022029900030223.

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SummaryDiscontinuous PAGE at alkaline and acid pH, polyacrylamide gel isoelectric focusing, two dimensional electrophoresis and immunoblotting have been used to study the heterogeneity of sheep caseins. Three main phenotypes were selected either because of mobility at alkaline and acid pH of the individual αs components or because of their relative intensity. On electrophoresis at alkaline pH, one phenotype showed two distinct bands of lower electrophoretic mobility than β,- and β2-caseins. A detailed study of these components using immunospecific detection with β-casein antiserum showed that these minor components of ovine casein may have a polypeptide chain similar to that of β1- and β2-caseins. Complete electrophoretic patterns of the casein components in some individual milks are also presented.

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Lenasi, Tina, Irena Rogelj, and Peter Dovc. "Characterization of equine cDNA sequences for αS1-, β- and κ-casein." Journal of Dairy Research 70, no. 1 (February 2003): 29–36. http://dx.doi.org/10.1017/s002202990200599x.

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Here we report the entire cDNA sequences for equine αS1-, β- and κ-casein. Based on interspecies comparison, nine exons were found in equine β-casein and five in κ-casein. In equine αS1-casein cDNA the exon 5 was missing, which resulted in the total of 18 exons instead of 19 theoretically possible exons in αS1-casein cDNA. Comparison of DNA sequences representing exon 5 in other species with corresponding equine genomic region confirmed the presence of cryptic exon in horse genomic DNA. Equine αS1-casein mRNA was present in three forms in the lactating mammary gland and we showed that the two shorter forms were produced by skipping either the exon 8 or exon 15. In horse, as in some other mammals, β- and κ-casein are considerably more conserved (sequence identity 53% to 59% and 57% to 67%, respectively) than αS1-casein which appears as the most variable casein among species (sequence identity 40% to 54%). Interestingly, horse caseins resemble human much more than bovine caseins which may also explain the high dietetic value of mares' milk.

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Pelmuş, Rodica Ştefania, Cristina Lazăr, M. L. Palade, Mariana Stancu, C. M. Rotar, and M. A. Gras. "Study on milk composition and milk protein distribution in Romanian Holstein cattle." Archiva Zootechnica 23, no. 1 (June 1, 2020): 13–21. http://dx.doi.org/10.2478/azibna-2020-0002.

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AbstractThe aim of this study was to determine milk quality indices as well as the milk protein composition in Romanian Holstein cattle raised under the conditions of experimental farm of INCDBNA-IBNA. The study was carried out on 22 milk samples. The types of different milk proteins were identified by SDS-PAGE technique. Sampling day and milk chemical composition were performed during the milking period of studied cattle. The quality indices were breed-specific for protein (3.38%) and higher for fat (4.39%).Milk proteins analysis of Romanian Holstein cattle separated by SDS-PAGE electrophoresis showed the presence of four major caseins (αs1-, αs2-, β- and k-casein) and two whey proteins (β-lactoglobulin, α-lactalbumin). The caseins accounted 77.28% of the total milk proteins, while the major proteins (β-lactoglobulin, α-lactalbumin) from the whey represented 22.72% of the total proteins. αs1-casein + αs2-casein had a higher expression (36.01%) followed by β-casein (31.45%), β-lactoglobulin (18.16%), k-casein (9.82%) and α-lactalbumin (4.56%). The most of milk samples was characterized by a medium expression level of both caseins and whey proteins

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Kaminarides, Stelios E., and Emmanuel M. Anifantakis. "Comparative study of the separation of casein from bovine, ovine and caprine milks using HPLC." Journal of Dairy Research 60, no. 4 (November 1993): 495–504. http://dx.doi.org/10.1017/s0022029900027850.

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SummaryThe separation of cows', sheep's and goats' milk casein components by HPLC on a strong anion-exchange (P.L-SAX 8μ 1000A) column is described. During HLPC, whole caseins of the three kinds of milk behaved differently from conventional separations. The casein components of the three kinds of milk were well resolved under the Chromatographie conditions used. HPLC resolved the κ-caseins better than did ion-exchange chromatography on DEAE cellulose, and was particularly efficient in the case of goats' milk. Goats' and sheep's milks had almost similar Chromatographie profiles but these differed considerably from that of cows' milk. Caseins from the sheep and the goat were also similar in that a shallower NaCl gradient was required for the separation of casein components than for cows' milk.

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BELLOQUE, JOSEFINA, and MERCEDES RAMOS. "Determination of the casein content in bovine milk by 31P-NMR." Journal of Dairy Research 69, no. 3 (August 2002): 411–18. http://dx.doi.org/10.1017/s0022029902005630.

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The relative proportion of caseins to total protein is a parameter that can be used to control the protein quality in standardised milk, an increasing tendency in dairy industries. 31P-NMR was used to analyse the casein content of milk, by the quantitation of the area under the resonances belonging to SerP, and using methylenediphosphonic acid as internal standard. This procedure yielded good results, as similar values of caseins were obtained from N Kjeldahl and NMR analysis for slightly heated milk samples. Heating at 95 °C for 15 min did not alter the casein content results. Casein content of raw, pasteurised and UHT milks (25·6±1·4, 26·4±1·8, 25·5±1·6 g casein/l milk, respectively), obtained by NMR, were not significantly different, giving an average of 25·8±1·6 g casein/l for bulk liquid milk. This work concluded that 31P-NMR could be used as an alternative method to determine casein in raw, pasteurised, dry and UHT milks.

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Cook, Tim. "Review of Cashin, Joan E., ed. 2018. War Matters: Material Culture in the Civil War Era. Chapel Hill: University of North Carolina Press." Material Culture Review 87 (July 27, 2020): 50–51. http://dx.doi.org/10.7202/1070685ar.

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Mikkelsen, Jan, Peter Højrup, and Jens Knudsen. "Purification of goats' milk casein by reversed-phase high-performance liquid chromatography and identification of αs1-casein." Journal of Dairy Research 54, no. 3 (August 1987): 361–67. http://dx.doi.org/10.1017/s002202990002553x.

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SummaryGoats’ milk caseins were separated into four components in a single run using reversed-phase gradient high-performance liquid chromatography. The purity of the isolated components was checked by sodium dodecyl sulphate polyacrylamide gel electrophoresis, amino acid analysis and determination of the N-terminal residue. By a comparison with previously published results for goats’ milk caseins the four peaks were identified as κ-, αs1-, αs2- and β-casein. In order to confirm the existence of αsl-casein in goats’ milk, this component was sequenced for 44 steps, revealing a sequence homologous to bovine αsl-casein and almost identical to the N-terminal sequence previously published by Boulanger et al. (1984).

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Stasiuk, Susan J., Emma L. Summers, and Jerome Demmer. "Cloning of a marsupial k-casein cDNA from the brushtail possum (Trichosurus vulpecula)." Reproduction, Fertility and Development 12, no. 4 (2000): 215. http://dx.doi.org/10.1071/rd99036.

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The main role of κ-casein in milk is to stabilize the formation of casein micelles. Although marsupial milk contains casein micelles, κ-casein had not been identified in any species. In these experiments, the first marsupial κ-casein has been prepared as enriched casein fractions and the cDNA cloned from the brushtail possum (Trichosurus vulpecula). Possum κ-casein is a 158 amino acid peptide that shares low amino acid sequence identity (20–30%) with that of eutherian κ-caseins. In the gut of suckling young, casein micelles clot when κ-casein is cleaved by chymosin at a specific site. Eutherian κ-casein sequences are classified according to the sequence of the chymosin cleavage site: Phe-Met, Phe-Ile or Phe-Leu. Possum κ-casein appears to form a separate class, with a putative chymosin cleavage site of Phe-Ala, which is different from that found in eutherian mammals. Other features of κ-caseins, such as the location of the N-terminal cysteine, solubility in the presence of calcium, and the O-glycosylation sites on threonine residues in the C-terminus of the molecule, are conserved in the possum sequence. The κ-casein gene was expressed throughout lactation in the mammary gland, and although mRNA levels of κ-, α- and β-casein varied between animals there appeared to be a correlation in the expression of these genes within an individual animal. This suggests that a common transcription regulatory region may be controlling expression of all three genes in the possum.

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Kaskous, Shehadeh. "A1- and A2-Milk and Their Effect on Human Health." Journal of Food Engineering and Technology 9, no. 1 (June 15, 2020): 15–21. http://dx.doi.org/10.32732/jfet.2020.9.1.15.

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Milk proteins are a heterogeneous group of polymeric compounds that have a wide range of different molecular structures and properties. They occur as caseins, whey proteins, enzymes, minor proteins and nitrogen compounds. Caseins constitute about 80% of the total proteins of cow’s milk. β-casein is an important part of the caseins, which makes up about 37% of the total caseins. Within β-casein, there are a number of variants which are genetically determined. However, there are thirteen genetic variants of β-casein found in cow´s milk. A1 and A2 are the most common variants, which are called A1 β-casein (A1-milk) and A2 β-casein (A2-milk). The only difference between A1- and A2-milk is a difference in the 67th amino acid in the chain. At this position, A2-milk has a proline amino acid, while A1-milk has histidine amino acid. Several studies have reported that cow’s milk with a dominant or singular A2-milk may be healthier than A1-milk. These studies are based on digestion of A1-milk which lead to release β-casomorphin-7 (BCM-7). Subsequently increase inflammation, Type-1-diabetes, heart disease, autism, gastrointestinal discomfort and other disease in the consumer. For this reason, there is a growing global interest in A2-milk. In conclusion, the effects of A1-milk compared to A2-milk on human health show mixed results. On the basis of the available results, we cannot conclusively assess the health effects of A1-milk and A2-milk. Therefore, further investigations are needed.

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Dalgleish, Douglas G. "Analysis by fast protein liquid chromatography of variants of κ-casein and their relevance to micellar structure and renneting." Journal of Dairy Research 53, no. 1 (February 1986): 43–51. http://dx.doi.org/10.1017/s002202990002464x.

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SUMMARYFast protein liquid chromatography was used to study the κ-casein fraction of casein micelles from bulk milk and from milk from individual animals homozygous for κ-caseins A and B. The extent of glycosylation of the κ-casein appeared to have no effect on its distribution in casein micelles of different sizes, nor did it affect the rate at which κ-casein was destroyed during renneting. The rate of breakdown of κ-casein during renneting was also almost independent of micellar size. The results may indicate a difference between methods which analyse for intact κ-casein or for the product macropeptide during renneting.

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Symcox, Linda. "Edward J. Cashin, Beloved Bethesda: A History of George Whitefield's Home for Boys, 1740–2000. Macon, GA: Mercer University Press, 2001. 288pp. Cloth $35.00." History of Education Quarterly 43, no. 1 (2003): 117–20. http://dx.doi.org/10.1017/s0018268000017416.

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Browne, Ray B. "Billy Benson's Civil War Book: Memoirs of a Confederate Scout and Sharpshooter by Susan Williams Benson, Editor, with New Introduction by Edward J. Cashin." Journal of American Culture 30, no. 3 (September 2007): 335–36. http://dx.doi.org/10.1111/j.1542-734x.2007.00564.x.

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MOLINA, ELENA, MERCEDES DE FRUTOS, and MERCEDES RAMOS. "Capillary electrophoresis characterization of the casein fraction of cheeses made from cows', ewes' and goats' milks." Journal of Dairy Research 67, no. 2 (May 2000): 209–16. http://dx.doi.org/10.1017/s0022029900004167.

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Casein fractions and their breakdown products in Iberico-type cheeses made from the milk of cows, ewes or goats were analysed by capillary electrophoresis in order to characterize them. The actions of plasmin and chymosin on caseins were evaluated by comparing the electropherograms of caseins from milk and from cheese, both with and without treatment with plasmin. Characteristic capillary electrophoresis patterns were obtained for cheeses made from the milk of each of the three species, and the main components were identified. Caprine para-κ-casein and bovine β-caseins, eluting at the first and at the last part of the electropherogram respectively, were found to be indicative of the presence of the milks of these species.

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Fatombi, J. K., T. Aminou, B. Lartiges, N. Topanou, and R. G. Josse. "Interaction of Cocos nucifera cream casein with humic acid suspensions." Water Science and Technology 66, no. 2 (July 1, 2012): 345–51. http://dx.doi.org/10.2166/wst.2012.190.

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Two caseins labelled as CaSMG (casein without fats) and CaMG (casein with fats) were extracted from coconut cream. Both caseins were used as coagulants for the aggregation of humic acid (HA) particles in synthetic water at pH = 6 during the jar-test essays. The optimum dosage of CaMG or CaSMG and the residual turbidities of treated water obtained depend on the type of used casein (CaMG or CaSMG) and the concentration of particles in solution. The optimal doses of CaMG and CaSMG are respectively 280 and 180 mg/L for solution S1 (HA aqueous solution at 15 mg/L), and then 340 and 240 mg/L for solution S2 (HA aqueous solution at 25 mg/L). The residual turbidities of treated water are respectively 6.88 and 3.85 NTU for solution S1 and 4.52 and 2.53 NTU for solution S2. The collected sediment volumes are respectively 1.2 and 1.5 mL for solutions S1 and S2. The electrophoretic mobility measurement and transmission electron microscopy images of flocs formed during the flocculation essays suggest that both caseins operate through both mechanisms (charge neutralisation and bridging process mechanism), this last one seems to be predominant. The aggregates formed are the large clusters and result from adsorption of HA particles by the casein molecules.

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Bonsing, John, Jennifer M Ring, A. Francis Stewart, and Antony G Mackinlay. "Complete Nucleotide Sequence of the Bovine ß-casein Gene." Australian Journal of Biological Sciences 41, no. 4 (1988): 527. http://dx.doi.org/10.1071/bi9880527.

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The !'i-casein gene is a member of a small gene family encoding the calcium-sensitive caseins, which are specifically synthesized and secreted by the mammary gland during lactation in response to both peptide and steroid hormones. The caseins are involved in the transport of calcium phosphate in milk, which is important for bone development in the infant mammal. We report here the organization and complete DNA sequence of the 8�5 kb long bovine !'i-casein gene. Comparison with the rat !'i-casein gene reveals that the exons of both genes correspond exactly. The 5' flanking sequences of all Ca-sensitive casein genes are conserved within the proximal 200 bp and contain several elements that probably function as cis-acting regulatory elements, including an octamer-like motif, an SV40-type core enhancer and a sequence that appears to be common to all lactoprotein genes. The latter sequence is flanked on either side by 12 bp direct repeats. These direct repeats are themselves each part of sequences that display two-fold symmetry. The first 30 nucleotides of the 3' flanking regions in the bovine and rat !'i-caseins are well conserved, indicating that they are likely to be involved in the mechanism of 3' end processing of the primary transcript.

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Journal articles on the topic 'Cashin'

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