Journal articles on the topic 'Lactoglobulin'
Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles
Consult the top 50 journal articles for your research on the topic 'Lactoglobulin.'
Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.
You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.
Browse journal articles on a wide variety of disciplines and organise your bibliography correctly.
ZAPPACOSTA, FRANCESCA, ALDO DI LUCCIA, LUIGI LEDDA та FRANCESCO ADDEO. "Identification of C-terminally truncated forms of β-lactoglobulin in whey from Romagnola cows' milk by two dimensional electrophoresis coupled to mass spectrometry". Journal of Dairy Research 65, № 2 (1998): 243–52. http://dx.doi.org/10.1017/s0022029997002859.
Full textCollet, C., R. Joseph та K. Nicholas. "A marsupial β-lactoglobulin gene: characterization and prolactin-dependent expression". Journal of Molecular Endocrinology 6, № 1 (1991): 9–16. http://dx.doi.org/10.1677/jme.0.0060009.
Full textSawyer, Lindsay, Sharon Brownlow, Igor Polikarpov та Su-Ying Wu. "β-Lactoglobulin". International Dairy Journal 8, № 2 (1998): 65–72. http://dx.doi.org/10.1016/s0958-6946(98)00021-1.
Full textJaved, N. H., Y. Z. Wang, and H. J. Cooke. "Neuroimmune interactions: role for cholinergic neurons in intestinal anaphylaxis." American Journal of Physiology-Gastrointestinal and Liver Physiology 263, no. 6 (1992): G847—G852. http://dx.doi.org/10.1152/ajpgi.1992.263.6.g847.
Full textBai, Lanlan, Yun Gao, Jiajia Wang та ін. "Detection of β-Lactoglobulin by a Porous Silicon Microcavity Biosensor Based on the Angle Spectrum". Sensors 22, № 5 (2022): 1912. http://dx.doi.org/10.3390/s22051912.
Full textFOLCH, JOSEP M., PETER DOVČ та JUAN F. MEDRANO. "Differential expression of bovine β-lactoglobulin A and B promoter variants in transiently transfected HC11 cells". Journal of Dairy Research 66, № 4 (1999): 537–44. http://dx.doi.org/10.1017/s0022029999003787.
Full textHirota, Kouichi, Seiichi Hashida, Eiji Ishikawa та Masayuki Totani. "Sensitive Enzyme Immunoassay for Anti-β-Lactoglobulin IgG in Serum". Annals of Clinical Biochemistry: International Journal of Laboratory Medicine 35, № 5 (1998): 649–55. http://dx.doi.org/10.1177/000456329803500509.
Full textRobitaille, Gilles. "Influence of κ-casein and β-lactoglobulin genetic variants on the heat stability of milk". Journal of Dairy Research 62, № 4 (1995): 593–600. http://dx.doi.org/10.1017/s0022029900031320.
Full textLiu, Ying, Ju-Jean Shaw, Harold E. Swaisgood та Jonathan C. Allen. "Bioavailability of Oil-Based and β-Lactoglobulin-Complexed Vitamin A in a Rat Model". ISRN Nutrition 2013 (19 лютого 2013): 1–8. http://dx.doi.org/10.5402/2013/270580.
Full textWang, Bixuan, Jingyi Hong, Chun Liu, Liying Zhu та Ling Jiang. "An Electrochemical Molecularly Imprinted Polymer Sensor for Rapid β-Lactoglobulin Detection". Sensors 21, № 24 (2021): 8240. http://dx.doi.org/10.3390/s21248240.
Full textMcSwiney, Mary, Harjinder Singh, Osvaldo Campanella та Lawrence K. Creamer. "Thermal gelation and denaturation of bovine β-lactoglobulins A and B". Journal of Dairy Research 61, № 2 (1994): 221–32. http://dx.doi.org/10.1017/s0022029900028235.
Full textZhou, Xinhui, Cuina Wang, Xiaomeng Sun, Zixuan Zhao та Mingruo Guo. "Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin". Molecules 25, № 16 (2020): 3637. http://dx.doi.org/10.3390/molecules25163637.
Full textSANNIER, FRÉDÉRIC, STÉPHANIE BORDENAVE та JEAN-MARIE PIOT. "Purification of goat β-lactoglobulin from whey by an ultrafiltration membrane enzymic reactor". Journal of Dairy Research 67, № 1 (2000): 43–51. http://dx.doi.org/10.1017/s0022029999004033.
Full textHoffmann, Marion A. M., Sebastianus P. F. M. Roefs, Marleen Verheul, Peter J. J. M. van Mil та Kees G. De Kruif. "Aggregation of β-lactoglobulin studied by in situ light scattering". Journal of Dairy Research 63, № 3 (1996): 423–40. http://dx.doi.org/10.1017/s0022029900031939.
Full textBayraktar, M. "Molecular characterization of Kappa-casein and β-lactoglobulin genes in Anatolian Black cattle and Holstein breeds". Arquivo Brasileiro de Medicina Veterinária e Zootecnia 74, № 1 (2022): 133–40. http://dx.doi.org/10.1590/1678-4162-12497.
Full textCoussons, P. J., N. C. Price, S. M. Kelly, B. Smith та L. Sawyer. "Transglutaminase catalyses the modification of glutamine side chains in the C-terminal region of bovine β-lactoglobulin". Biochemical Journal 283, № 3 (1992): 803–6. http://dx.doi.org/10.1042/bj2830803.
Full textEpishko, O. A., V. V. Peshko, and N. N. Peshko. "ASSOCIATION OF POLYMORPHISM OF THE BETA-LACTOGLOBULIN GENE FROM MILK PRODUCTION OF COWS OF THE BELARUSIAN BLACK-MOTLEY BREED." Animal Breeding and Genetics 53 (April 27, 2017): 215–21. http://dx.doi.org/10.31073/abg.53.29.
Full textXu, Amy Y., Laurence D. Melton, Geoffrey B. Jameson, Martin A. K. Williams, and Duncan J. McGillivray. "Structural mechanism of complex assemblies: characterisation of beta-lactoglobulin and pectin interactions." Soft Matter 11, no. 34 (2015): 6790–99. http://dx.doi.org/10.1039/c5sm01378j.
Full textBoye, Joyce I., Ashraf A. Ismail та Inteaz Alli. "Effects of physicochemical factors on the secondary structure of β-lactoglobulin". Journal of Dairy Research 63, № 1 (1996): 97–109. http://dx.doi.org/10.1017/s0022029900031575.
Full textde LUIS, R., M. D. PÉREZ, L. SÁNCHEZ, M. LAVILLA та M. CALVO. "Development of Two Immunoassay Formats To Detect β-Lactoglobulin: Influence of Heat Treatment on β-Lactoglobulin Immunoreactivity and Assay Applicability in Processed Food". Journal of Food Protection 70, № 7 (2007): 1691–97. http://dx.doi.org/10.4315/0362-028x-70.7.1691.
Full textOTANI, Hajime, Takashi UCHIO, and Fumisaburo TOKITA. "Antigenic reactivities of chemically modified .BETA.-lactoglobulins with antiserum to bovine .BETA.-lactoglobulin." Agricultural and Biological Chemistry 49, no. 9 (1985): 2531–36. http://dx.doi.org/10.1271/bbb1961.49.2531.
Full textOtani, Hajime, Takashi Uchio та Fumisaburo Tokita. "Antigenic Reactivities of Chemically Modified β-Lactoglobulins with Antiserum to Bovine β-Lactoglobulin". Agricultural and Biological Chemistry 49, № 9 (1985): 2531–36. http://dx.doi.org/10.1080/00021369.1985.10867140.
Full textLOPEZ-FANDIÑO, ROSINA, NIEVES CORZO, MAR VILLAMIEL, TERESA DELGADO, AGUSTIN OLANO, and MERCEDES RAMOS. "Assessment of Quality of Commercial UHT Milks by Chromatographic and Electrophoretic Methods." Journal of Food Protection 56, no. 3 (1993): 263–64. http://dx.doi.org/10.4315/0362-028x-56.3.263.
Full textPérez, M. Dolores, Pilar Puyol, José Manuel Ena та Miguel Calvo. "Comparison of the ability to bind lipids of β-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species". Journal of Dairy Research 60, № 1 (1993): 55–63. http://dx.doi.org/10.1017/s0022029900027345.
Full textAzdad, Ouarda, Najlae Mejrhit, and Lotfi Aarab. "The effect of treatments on the allergenicity of ß-lactoglobulin in Moroccan population." Nutrition & Food Science 48, no. 4 (2018): 538–48. http://dx.doi.org/10.1108/nfs-11-2017-0250.
Full textMORKÛNIENË, K., I. MICEIKIENË, S. KERZIENË, R. BIZIENË, and R. MISEIKIENË. "Genetic diversity of milk protein beta-lactoglobulin and association with production traits genomic values among Holstein cattle." Indian Journal of Animal Sciences 88, no. 11 (2018): 1289–93. http://dx.doi.org/10.56093/ijans.v88i11.85058.
Full textIkonen, Tiina, Matti Ojala та Eeva-Liisa Syväoja. "Effects of composite casein and β-lactoglobulin genotypes on renneting properties and composition of bovine milk by assuming an animal model". Agricultural and Food Science 6, № 4 (1997): 283–94. http://dx.doi.org/10.23986/afsci.72791.
Full textOlsen, Karsten, Bo B. Jespersen та Vibeke Orlien. "Changes of pH inβ-Lactoglobulin andβ-Casein Solutions during High Pressure Treatment". Journal of Spectroscopy 2015 (2015): 1–6. http://dx.doi.org/10.1155/2015/935901.
Full textSingina, G. N., P. V. Sergiev, A. V. Lopukhov, et al. "Production of a Cloned Offspring and CRISPR/Cas9 Genome Editing of Embryonic Fibroblasts in Cattle." Doklady Biochemistry and Biophysics 496, no. 1 (2021): 48–51. http://dx.doi.org/10.1134/s1607672921010099.
Full textVelmala, Riikka, Esa A. Mäntysaari та Asko Mäki-Tanila. "Molecular genetic polymorphism at the κ-casein and β-lactoglobulin loci in Finnish dairy hulls". Agricultural and Food Science 2, № 5 (1993): 431–35. http://dx.doi.org/10.23986/afsci.72669.
Full textMonti, Daria Maria, Domenico Loreto, Ilaria Iacobucci та ін. "Protein-Based Delivery Systems for Anticancer Metallodrugs: Structure and Biological Activity of the Oxaliplatin/β-Lactoglobulin Adduct". Pharmaceuticals 15, № 4 (2022): 425. http://dx.doi.org/10.3390/ph15040425.
Full text&NA;. "Modified ??-lactoglobulin blocks HIV." Inpharma Weekly &NA;, no. 1026 (1996): 9. http://dx.doi.org/10.2165/00128413-199610260-00021.
Full textAkita, E. M., та S. Nakai. "Lipophilization of β-Lactoglobulin". Canadian Institute of Food Science and Technology Journal 20, № 5 (1987): 316. http://dx.doi.org/10.1016/s0315-5463(87)71249-8.
Full textDonald, Athene M. "Aggregation in β-lactoglobulin". Soft Matter 4, № 6 (2008): 1147. http://dx.doi.org/10.1039/b800106e.
Full textBonomi, Francesco, Alessandro Fiocchi, Hanne Frøkiær та ін. "Reduction of immunoreactivity of bovine β-lactoglobulin upon combined physical and proteolytic treatment". Journal of Dairy Research 70, № 1 (2003): 51–59. http://dx.doi.org/10.1017/s0022029902005678.
Full textBrodziak, Aneta, Jolanta Król, Anna Litwińczuk, and Anna Wolanciuk. "Correlations between the content of selected whey proteins in cow milk." Roczniki Naukowe Polskiego Towarzystwa Zootechnicznego 13, no. 1 (2017): 33–45. http://dx.doi.org/10.5604/01.3001.0013.5306.
Full textRocha, Thales L., Sharon Brownlow, Keith N. Saddler, Linda A. Fothergill-Gilmore та Lindsay Sawyer. "New crystal form of β-lactoglobulin". Journal of Dairy Research 63, № 4 (1996): 575–84. http://dx.doi.org/10.1017/s0022029900032118.
Full textLangley, Keith R., David Millard, and E. William Evans. "Determination of tensile strength of gels prepared from fractionated whey proteins." Journal of Dairy Research 53, no. 2 (1986): 285–92. http://dx.doi.org/10.1017/s0022029900024882.
Full textROCHA, Thales L., Gary PATERSON, Kay CRIMMINS, Alan BOYD, Lindsay SAWYER та Linda A. FOTHERGILL-GILMORE. "Expression and secretion of recombinant ovine β-lactoglobulin in Saccharomyces cerevisiae and Kluyveromyces lactis". Biochemical Journal 313, № 3 (1996): 927–32. http://dx.doi.org/10.1042/bj3130927.
Full textRodríguez-Amigo, Beatriz, Cormac Hally, Núria Roig-Yanovsky та ін. "A Double Payload Complex between Hypericin and All-trans Retinoic Acid in the β-Lactoglobulin Protein". Antibiotics 11, № 2 (2022): 282. http://dx.doi.org/10.3390/antibiotics11020282.
Full textKADDOURI, H., S. MIMOUN, K. E. EL-MECHERFI, A. CHEKROUN, O. KHEROUA та D. SAIDI. "Impact of γ-Radiation on Antigenic Properties of Cow's Milk β-Lactoglobulin". Journal of Food Protection 71, № 6 (2008): 1270–72. http://dx.doi.org/10.4315/0362-028x-71.6.1270.
Full textOsborne, Rebecca, Michael Howell, A. John Clark та Kevin R. Nicholas. "Hormone-dependent expression of the ovine β-lactoglobulin gene". Journal of Dairy Research 62, № 2 (1995): 321–29. http://dx.doi.org/10.1017/s0022029900031010.
Full textSladic, Dusan, Irena Novakovic, Zoran Vujcic, et al. "Protein covalent modification of biologically active quinones." Journal of the Serbian Chemical Society 69, no. 11 (2004): 901–7. http://dx.doi.org/10.2298/jsc0411901s.
Full textJongberg, Sisse, Michael Rasmussen, Leif H. Skibsted, and Karsten Olsen. "Detection of Advanced Glycation End-Products (AGEs) During Dry-State Storage of ?-Lactoglobulin/Lactose." Australian Journal of Chemistry 65, no. 12 (2012): 1620. http://dx.doi.org/10.1071/ch12442.
Full textLoch, Joanna I., Jakub Barciszewski, Joanna Śliwiak та ін. "New ligand-binding sites identified in the crystal structures of β-lactoglobulin complexes with desipramine". IUCrJ 9, № 3 (2022): 386–98. http://dx.doi.org/10.1107/s2052252522004183.
Full textKuwata, K., H. Li, H. Yamada та ін. "Folding process of β-lactoglobulin". Seibutsu Butsuri 39, supplement (1999): S109. http://dx.doi.org/10.2142/biophys.39.s109_3.
Full textKuwata, K., Y. Goto, M. Hoshino, and Roder Heinrich. "Folding intermediate of beta-lactoglobulin." Seibutsu Butsuri 40, supplement (2000): S162. http://dx.doi.org/10.2142/biophys.40.s162_2.
Full textMercad-Prieto, Ruben, William R. Paterson, and D. Ian Wilson. "Caustic-induced gelation of -lactoglobulin." International Journal of Food Science & Technology 43, no. 8 (2008): 1379–86. http://dx.doi.org/10.1111/j.1365-2621.2007.01643.x.
Full textBatt, Carl A., John Brady та Lindsay Sawyer. "Design improvements of β-lactoglobulin". Trends in Food Science & Technology 5, № 8 (1994): 261–65. http://dx.doi.org/10.1016/0924-2244(94)90019-1.
Full textBotelho, Michelle M., Vera L. Valente-Mesquita, Kesley M. G. Oliveira, Igor Polikarpov та Sérgio T. Ferreira. "Pressure denaturation of β-lactoglobulin". European Journal of Biochemistry 267, № 8 (2000): 2235–41. http://dx.doi.org/10.1046/j.1432-1327.2000.01226.x.
Full text