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Journal articles on the topic 'Phosvitine'

Author: Grafiati

Published: 4 June 2021

Last updated: 15 February 2022

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1

Tran, Khoa Nguyen, and Van Song Toan Vo. "Evaluation of the purification process of phosvitin extracted from chicken egg yolk using liquid chromatography." Can Tho University Journal of Science 13, no. 2 (July 29, 2021): 77–84. http://dx.doi.org/10.22144/ctu.jen.2021.033.

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Phosvitin from chicken egg yolk, known as a phosphoglycoprotein, owns a very strong metal chelating property due to its polyanionic character. This study aimed to evaluate the factors affecting the purification process and suitable conditions to increase phosvitin’s purity. Phosvitin was separated from yolk granules by using 10% of NaCl solution in 0.05 M NaOH solution and heat treatment which removes lipoprotein from the extracted solution. The highest phosphorus content (58.14 mg) and phosphorus recovery rate (32.4%) were obtained at thermal treatment of 30℃ for 30 minutes. In addition, phosvitin was purified using anion-exchange chromatography (AEC) and gel-filtration chromatography (GFC). The fraction 1 (F1) obtained from AEC using UNO-Sphere Q at pH 8 had the recovery rate of phosvitin approximately 72.73%. Furthermore, fraction F1 was separated on GFC to obtain two main sub-fractions (F1 and F2). Sub-fraction F1 from gel filtration was composed mostly of β-phosvitin with a high recovery rate (81.93%) while F2 was dominant with α-phosvitin in a lower phosvitin recovery rate (16.89%). These findings will provide useful information for further researches on other properties of phosvitin so that it can be applied widely in human needs.

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2

Wallace, R. A., and J. P. Morgan. "Chromatographic resolution of chicken phosvitin. Multiple macromolecular species in a classic vitellogenin-derived phosphoprotein." Biochemical Journal 240, no. 3 (December 15, 1986): 871–78. http://dx.doi.org/10.1042/bj2400871.

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Chicken phosvitin was prepared from egg yolk by a variety of published methods, including a modification of our own original procedure. Yolk granules and all phosvitin preparations have been previously found to contain major phosphoproteins at Mr 40,000 and 33,000 and minor satellite components when electrophoresed on polyacrylamide gradient gels and stained with Stains-all. However, only our current preparation contained three additional phosphoproteins (Mr 18,000, 15,000 and 13,000) that are also present in yolk granules. Our current phosvitin preparation also appeared to have additional components when compared with other preparations by size-exclusion and anion-exchange chromatography. Particularly complex but entirely reproducible patterns were obtained by hydrophobic-interaction chromatography. However, a cross-referencing of fractions eluted by size-exclusion chromatography to the other procedures employed, including gel electrophoresis, reinforced the notion that unfractionated chicken phosvitin contains at least five major components, designated B, C, E1, E2 and F for the Mr 40,000, 33,000, 15,000, 18,000, and 13,000 phosphoproteins, respectively. Stoichiometric considerations lead us to suggest that vitellogenin I gives rise to phosvitins C and F, vitellogenin II gives rise to phosvitin B, and vitellogenin III gives rise to either phosvitin E1 or E2, but not both. Thus, a fourth, as yet undetected, vitellogenin may exist for the chicken.

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3

Shipman, Richard D., Sean D. Doering, Jack R. Hemsath, Eun Joo Lee, and Jennifer E. Grant. "Activity of Phosvitin in Hydroxyapatite Acid-Damage Immersion and Antimicrobial Assays." Biochemistry Research International 2020 (October 24, 2020): 1–10. http://dx.doi.org/10.1155/2020/8831311.

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Phosvitin, the most highly phosphorylated metal-binding protein found in nature, binds more than 100 calcium ions, and has been identified as an agent that could be used to generate biomineralization scaffolds. Because of published reports describing phosvitin’s affinity for calcium and potential antibiotic activity, this study was undertaken in order to evaluate phosvitin for both antibiotic activity against common microorganisms and the ability to protect hydroxyapatite surfaces from acid damage. To more clearly define its antibiotic action, the effects of phosvitin on Micrococcus luteus, P. mirabilis, B. cereus, E. coli, and S. epidermidis were evaluated. In both Kirby–Bauer tests and liquid culture growth inhibition assays, phosvitin inhibited M. luteus, a microorganism that thrives in the human mouth, but not the other bacteria tested. The MIC of phosvitin was determined to be 31.3 μg/mL when delivered in 1 mM CaCl2 but was 0.5 mg/mL in the absence of added calcium. Expanding on the potential impacts of phosvitin on the mouth, its action was evaluated in a model of tooth decay represented by acid-damaged hydroxyapatite discs. SEM, AFM, and FAAS analyses revealed that pretreatment of discs with phosvitin modulated the damage-induced morphology and topography changes associated with acid-damaged discs.

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4

Liu, Jian Guo, Xue Fang Zhang, and Jing Liu. "Isolation and Characterization of Phosvitin from Chicken Egg Yolk." Advanced Materials Research 554-556 (July 2012): 1415–18. http://dx.doi.org/10.4028/www.scientific.net/amr.554-556.1415.

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In the present work, a new dialysis process was proposed to isolate phosvitin from chicken egg yolk, which consists of NaCl precipitation, heat treatment and dialysis. The effects of several key operating parameters on the purity of phosvitin were examined. Under optimized conditions, the phosvitin purity obtained was about 86.3%, with a yield of 87.2%. The resulting phosvitin product had β-sheet of 78.5% at pH 2.0, consistent with the literature value. This shows that the purified phosvitin folded with a reasonable secondary structure.

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5

Giarratano, Mélanie, Pauline Duffuler, Julien Chamberland, Guillaume Brisson, James D. House, Yves Pouliot, and Alain Doyen. "Combination of High Hydrostatic Pressure and Ultrafiltration to Generate a New Emulsifying Ingredient from Egg Yolk." Molecules 25, no. 5 (March 5, 2020): 1184. http://dx.doi.org/10.3390/molecules25051184.

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Egg yolk granule phosvitin (45 kDa) is a phosphoprotein known for its emulsifying properties. Recently, high hydrostatic pressure (HHP) treatment of granule induced the transfer of phosvitin to the soluble plasma fraction. This project evaluated the performance of the ultrafiltration (UF) used to concentrate phosvitin from the plasma fraction to produce a natural emulsifier. Phosvitin was characterized in plasma from a pressure-treated granule (1.73 ± 0.07% w/w) and in its UF retentate (26.00 ± 4.12% w/w). The emulsifying properties of both retentates were evaluated. The emulsion prepared with phosvitin-enriched retentate was more resistant to flocculation and creaming. Confocal laser scanning microscopy showed a network of aggregated protein similar to a gel, which encapsulated oil droplets in emulsions made with UF-retentate of plasma from pressure-treated granule. However, although sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) showed that β-phosvitin is recovered in the cream, it is difficult to attribute the improved emulsifying properties of the UF-retentate of plasma from pressure-treated granules only to phosvitin.

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6

Liu, Jian Guo, Chang Zhen Chen, and Jing Liu. "A Novel Dialysis Process to Isolate Phosvitin from Hen Egg Yolk." Advanced Materials Research 554-556 (July 2012): 1542–46. http://dx.doi.org/10.4028/www.scientific.net/amr.554-556.1542.

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The objective of this work is to develop a novel dialysis process for the isolation of phosvitin from hen egg yolk avoiding the use of organic solvents and polyvalent metals. This bioseparation process consists of NaCl precipitation, heat treatment and dialysis, which was proposed on the basis of the property difference (especially solubility and thermostability) among yolk proteins. The native molecular mass of the purified phosvitin estimated by fast protein liquid chromatography on a Superdex 75 column was about 165 kDa. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis showed two bands around 35 kDa. The nitrogen to phosphorus atomic ratio of the purified phosvitin was 2.8 ± 0.2, with a yield of 87.1%. The phosvitin product had α-helix of 36%, β-sheet of 28% and random coil of 36% at pH 7.0, consistent with the literature values. This shows that the purified phosvitin folded with a reasonable secondary structure.

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7

Chakrabarti, Subhadeep, Jiandong Ren, and Jianping Wu. "Phosvitin Derived Phospho-Peptides Show Better Osteogenic Potential than Intact Phosvitin in MC3T3-E1 Osteoblastic Cells." Nutrients 12, no. 10 (September 30, 2020): 2998. http://dx.doi.org/10.3390/nu12102998.

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Phosphorylated proteins from food sources have been investigated as regulators of bone formation with potential benefits in treating osteoporosis. Egg, a cheap and nutritious food, is also the source of various proteins and bioactive peptides with applications in human health. Egg yolk is rich in phosvitin, the most phosphorylated protein in nature. Phosvitin has been shown to improve bone health in experimental animals, although the molecular mechanisms and its specific effects on bone-forming osteoblastic cells are incompletely understood. Previous work in our group has identified pancreatin-generated phosvitin phospho-peptides (PPP) as a potential source for bioactive peptides. Given this background, we examined the roles of both phosvitin and PPP in the function of osteoblastic cells. Our results demonstrated their potential to improve bone health by promoting osteoblast differentiation and proliferation, suppressing osteoclast recruitment and the deposition of extracellular matrix, although PPP appeared to demonstrate superior osteogenic functions compared to phosvitin alone.

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8

Zhong, Q., X. Li, W. Hu, B. Zeng, R. Liang, H. Liu, Z. Li, and Z. Zhang. "Phosvitin phosphopeptide preparation using immobilised trypsin and enhancing calcium absorption in growing rats." Czech Journal of Food Sciences 34, No. 4 (September 5, 2016): 325–31. http://dx.doi.org/10.17221/425/2015-cjfs.

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We demonstrate a new, efficient method for the preparation of phosvitin phosphopeptides using immobilised-trypsin enzymolysis technology. Immobilised trypsin was prepared using a covalent binding method, and then was added to degrade egg yolk phosvitin for the production of phosphopeptides. In our results, the prepared immobilised trypsin demonstrated a higher hydrolysing activity toward phosvitin than free trypsin, and the hydrolysing activity was retained well even after trypsin was repeatedly used up to five times. Interestingly, the phosvitin phosphopeptides prepared with immobilised trypsin demonstrated a lower N/P ratio and a higher calcium-binding efficiency than those prepared with free trypsin. Furthermore, phosphopeptides significantly increased the rate of calcium absorption and serum calcium content in vivo. Based on these results, we conclude that trypsin immobilised onto chitosan has a greater phosvitin hydrolysing activity than free trypsin, and the prepared phosphopeptides can be used as a new calcium supplement to significantly increase calcium absorption in growing rats.

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9

Li, Mei, Xiang Li, Jing Li, Mei Lu, Xuebo Liu, and Xiang Duan. "Effects of multiple freeze–thaw treatments on physicochemical and biological activities of egg phosvitin and its phosphopeptides." Food & Function 9, no. 9 (2018): 4602–10. http://dx.doi.org/10.1039/c8fo01101j.

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10

Li, Songna, Feng Liu, Fuge Niu, Luping Gu, Yujie Su, and Yanjun Yang. "Purification of phosvitin phosphopeptides using macro-mesoporous TiO2." RSC Advances 5, no. 79 (2015): 64731–38. http://dx.doi.org/10.1039/c5ra12132a.

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11

Cui, Yanchun, Xiang Li, Mei Lu, Xuebo Liu, and Xiang Duan. "Role of polysaccharide conjugation in physicochemical and emulsifying properties of egg phosvitin and the calcium binding capacity of its phosphopeptides." Food & Function 10, no. 4 (2019): 1808–15. http://dx.doi.org/10.1039/c8fo02464b.

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12

Tazawa, Ichiro, Yasuo Inoue, Mariko Iwasaki, Sadako Inoue, Naoto Okumoto, and Fujio Hayashi. "Isolation and characterization of the major and the minor phosvitin from eight species (three genera) of salmonid fishes: Genus specific nature of the amino acid composition of the major phosvitin, and novel features of the chemical composition of the minor phosvitins." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 89, no. 3 (January 1988): 475–82. http://dx.doi.org/10.1016/0305-0491(88)90162-9.

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13

Li, Mei, Qinjun Zhang, Ruihan Wang, Mei Lu, Xueming Xu, Xuebo Liu, and Xiang Duan. "Effects of egg phosvitin on mucosal transcriptional profiles and luminal microbiota composition in murine colon." Food & Function 10, no. 5 (2019): 2805–16. http://dx.doi.org/10.1039/c9fo00074g.

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14

McCollum, Kathrin, Don Gregory, Brenda Williams, and George Taborsky. "Phosvitin isolation from fish eggs: Methodological improvements including ‘specific’ phosvitin precipitation with ferric ion." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 84, no. 2 (January 1986): 151–57. http://dx.doi.org/10.1016/0305-0491(86)90197-5.

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15

Fan, Jiadong, Yang Zhang, Nianjing Ji, Xiulan Duan, Hong Liu, Jiyang Wang, and Huaidong Jiang. "Hierarchical structures of self-assembled hybrid calcium carbonate: nucleation kinetic studies on biomineralization." CrystEngComm 17, no. 29 (2015): 5372–76. http://dx.doi.org/10.1039/c5ce00621j.

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16

Liang, Hongshan, Bin Zhou, Jing Li, Yaqiong Pei, and Bin Li. "Correction: Coordination-driven multilayer of phosvitin-polyphenol functional nanofibrous membranes: antioxidant and biomineralization applications for tissue engineering." RSC Advances 6, no. 109 (2016): 108151. http://dx.doi.org/10.1039/c6ra90108e.

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Correction for ‘Coordination-driven multilayer of phosvitin-polyphenol functional nanofibrous membranes: antioxidant and biomineralization applications for tissue engineering’ by Hongshan Liang et al., RSC Adv., 2016, 6, 98935–98944.

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17

Clark, Richard C. "The primary structure of avian phosvitins." International Journal of Biochemistry 17, no. 9 (January 1985): 983–88. http://dx.doi.org/10.1016/0020-711x(85)90243-5.

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18

Geladopoulos, Taxiarchis P., and Theodore G. Sotiroudis. "Interaction of aluminum ions with phosvitin." Journal of Inorganic Biochemistry 54, no. 4 (June 1994): 247–56. http://dx.doi.org/10.1016/0162-0134(94)80030-8.

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19

Tziboula, Athina, A. W. M. Sweetsur, and D. D. Muir. "Interactions between phosvitin and milk proteins." International Dairy Journal 4, no. 6 (January 1994): 491–501. http://dx.doi.org/10.1016/0958-6946(94)90021-3.

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20

Platt, Mark W., and Shlomo Rottem. "Phosvitin kinase activity in Acholeplasma axanthum." FEBS Letters 242, no. 1 (December 19, 1988): 97–100. http://dx.doi.org/10.1016/0014-5793(88)80993-1.

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21

Mulaa, Francis J., and Akintola A. Aboderin. "Two phosphoglycoproteins (phosvitins) from Kinixys erosa oocytes." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 103, no. 4 (December 1992): 1025–31. http://dx.doi.org/10.1016/0305-0491(92)90233-h.

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22

Jung, Samooel, Min-Gu Kang, Il-Suk Kim, Ki-Chang Nam, Dong-Uk Ahn, and Cheo-Run Jo. "Effect of Addition of Phosvitin and High Pressure Processing on Microbiological Quality and Lipid and Protein Oxidation of Minced Chicken Leg Meat." Korean Journal for Food Science of Animal Resources 32, no. 2 (April 30, 2012): 212–19. http://dx.doi.org/10.5851/kosfa.2012.32.2.212.

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23

Ma, Jie, Hongmiao Wang, Yongjun Wang, and Shicui Zhang. "Endotoxin-neutralizing activity of hen egg phosvitin." Molecular Immunology 53, no. 4 (April 2013): 355–62. http://dx.doi.org/10.1016/j.molimm.2012.09.006.

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24

Samaraweera, Himali, Wan-gang Zhang, Eun Joo Lee, and Dong U. Ahn. "Egg Yolk Phosvitin and Functional Phosphopeptides-Review." Journal of Food Science 76, no. 7 (August 1, 2011): R143—R150. http://dx.doi.org/10.1111/j.1750-3841.2011.02291.x.

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25

Dickinson, Eric, Valerie J. Pinfield, and David S. Horne. "On the “Anomalous” Adsorption Behavior of Phosvitin." Journal of Colloid and Interface Science 187, no. 2 (March 1997): 539–41. http://dx.doi.org/10.1006/jcis.1996.4695.

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26

Ren, Jiandong, and Jianping Wu. "Thermal-aided phosvitin extraction from egg yolk." Journal of the Science of Food and Agriculture 95, no. 13 (February 12, 2015): 2595–600. http://dx.doi.org/10.1002/jsfa.7073.

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27

Taborsky, George. "On the interaction of phosvitins with ferric ion: Solubility of the Fe(III)-phosphoprotein complex under acidic conditions is a function of the iron/phosphate ratio and the degree of phosvitin phosphorylation." Journal of Inorganic Biochemistry 44, no. 1 (October 1991): 65–77. http://dx.doi.org/10.1016/0162-0134(91)80062-m.

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28

Grogan, James, and George Taborsky. "Iron binding by phosvitins: variable mechanism of iron release by phosvitins of diverse species characterized by different degrees of phosphorylation." Journal of Inorganic Biochemistry 29, no. 1 (January 1987): 33–47. http://dx.doi.org/10.1016/0162-0134(87)80010-7.

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29

CHUNG, SIEW LIAN, and LES K. FERRIER. "Conditions Affecting Emulsifying Properties of Egg Yolk Phosvitin." Journal of Food Science 56, no. 5 (September 1991): 1259–62. http://dx.doi.org/10.1111/j.1365-2621.1991.tb04747.x.

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30

Tziboula, Athina, and Douglas G. Dalgleish. "Interaction of phosvitin with casein micelles in milk." Food Hydrocolloids 4, no. 2 (June 1990): 149–59. http://dx.doi.org/10.1016/s0268-005x(09)80015-5.

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31

Marcet, Ismael, Benjamin Paredes, and Mario Díaz. "Membrane technology purification of phosvitin from lipoprotein mixtures." New Biotechnology 29 (September 2012): S218. http://dx.doi.org/10.1016/j.nbt.2012.08.612.

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32

Grogan, James, Ata Shirazi, and George Taborsky. "Phosphorus nuclear magnetic resonance of diverse phosvitin species." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 96, no. 4 (January 1990): 655–63. http://dx.doi.org/10.1016/0305-0491(90)90210-k.

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33

Zhang, Xiaowei, Fang Geng, Xi Huang, and Meihu Ma. "Calcium binding characteristics and structural changes of phosvitin." Journal of Inorganic Biochemistry 159 (June 2016): 76–81. http://dx.doi.org/10.1016/j.jinorgbio.2016.02.001.

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34

Sun, Chen, Lili Hu, Shousheng Liu, Guobin Hu, and Shicui Zhang. "Antiviral activity of phosvitin from zebrafish Danio rerio." Developmental & Comparative Immunology 40, no. 1 (May 2013): 28–34. http://dx.doi.org/10.1016/j.dci.2012.12.009.

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35

Moon, Sun Hee, Jae Hoon Lee, Minhee Lee, Eunju Park, Dong Uk Ahn, and Hyun-Dong Paik. "Cytotoxic and antigenotoxic activities of phosvitin from egg yolk." Poultry Science 93, no. 8 (August 2014): 2103–7. http://dx.doi.org/10.3382/ps.2013-03784.

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36

SUZUKI, Takeshi, and Michizo SUYAMA. "Characterization of phosvitin and phosphopeptides of rainbow trout eggs." NIPPON SUISAN GAKKAISHI 51, no. 8 (1985): 1287–92. http://dx.doi.org/10.2331/suisan.51.1287.

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37

Byrne, B. Marion, Harry De Jong, Ronaldus A. M. Fouchier, David L. Williams, Max Gruber, and Geert Ab. "Rudimentary phosvitin domains in a minor chicken vitellogenin gene." Biochemistry 28, no. 6 (March 1989): 2572–77. http://dx.doi.org/10.1021/bi00432a034.

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38

Ding, Yunchao, Xuemei Liu, Lingzhen Bu, Hongyan Li, and Shicui Zhang. "Antimicrobial–immunomodulatory activities of zebrafish phosvitin-derived peptide Pt5." Peptides 37, no. 2 (October 2012): 309–13. http://dx.doi.org/10.1016/j.peptides.2012.07.014.

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39

CHUNG, SIEW LIAN, and LES K. FERRIER. "Heat Denaturation and Emulsifying Properties of Egg Yolk Phosvitin." Journal of Food Science 60, no. 5 (September 1995): 906–8. http://dx.doi.org/10.1111/j.1365-2621.1995.tb06258.x.

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40

Hu, Lili, Chen Sun, Jing Luan, Linlin Lu, and Shicui Zhang. "Zebrafish phosvitin is an antioxidant with non-cytotoxic activity." Acta Biochimica et Biophysica Sinica 47, no. 5 (April 6, 2015): 349–54. http://dx.doi.org/10.1093/abbs/gmv023.

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41

Kumar, Sumit, Gaëlle Creff, Christoph Hennig, André Rossberg, Robin Steudtner, Johannes Raff, Claude Vidaud, François R. Oberhaensli, Marie‐Yasmine Dechraoui Bottein, and Christophe Auwer. "How Do Actinyls Interact with Hyperphosphorylated Yolk Protein Phosvitin?" Chemistry – A European Journal 25, no. 53 (August 2019): 12332–41. http://dx.doi.org/10.1002/chem.201902015.

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42

Samaraweera, Himali, Sun Hee Moon, Eun Joo Lee, Jenifer Grant, Jordan Fouks, Inwook Choi, Joo Won Suh, and Dong U. Ahn. "Characterisation of phosvitin phosphopeptides using MALDI-TOF mass spectrometry." Food Chemistry 165 (December 2014): 98–103. http://dx.doi.org/10.1016/j.foodchem.2014.05.098.

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43

Lei, Bo, and Jianping Wu. "Purification of egg yolk phosvitin by anion exchange chromatography." Journal of Chromatography A 1223 (February 2012): 41–46. http://dx.doi.org/10.1016/j.chroma.2011.12.023.

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44

Ren, Jiandong, Qiyi Li, Marina Offengenden, and Jianping Wu. "Preparation and characterization of phosphopeptides from egg yolk phosvitin." Journal of Functional Foods 18 (October 2015): 190–97. http://dx.doi.org/10.1016/j.jff.2015.07.007.

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45

Egyh�zi, Endre, and Andrew Pigon. "Selective repression of RNA polymerase II by Microinjected phosvitin." Chromosoma 94, no. 5 (December 1986): 329–36. http://dx.doi.org/10.1007/bf00328632.

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46

Hu, Lili, Chen Sun, Shengnan Wang, Feng Su, and Shicui Zhang. "Lipopolysaccharide neutralization by a novel peptide derived from phosvitin." International Journal of Biochemistry & Cell Biology 45, no. 11 (November 2013): 2622–31. http://dx.doi.org/10.1016/j.biocel.2013.09.002.

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47

Hei, Yong-Jiang, Xunsheng Chen, Jack Diamond, and John H. McNeill. "Distribution of MAP kinase, S6 kinase, and casein kinase II in rat tissues: activation by insulin in spleen." Biochemistry and Cell Biology 72, no. 1-2 (January 1, 1994): 49–53. http://dx.doi.org/10.1139/o94-008.

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We examined the distribution of mitogen-activated protein (MAP) kinase, S6 kinase, and casein kinase II (CK-II) in the muscle, spleen, brain, and testes of Wistar rats. It was observed that spleen extracts contained the highest activity of all the kinases. Anion-exchange chromatography of spleen extracts by a MonoQ column resolved a single peak of myelin basic protein phosphotransferase activity that eluted after the usual position of the previously described p42 and p44 MAP kinases. Immunoblotting of the peak fractions with anti-MAP kinase antibody did not detect any immunoreactive bands that coincided with the activity peak, suggesting that the activity may represent a potentially novel MAP kinase. The MonoQ fractionation also resolved a single peak of phosvitin phosphotransferase activity which coincided with the intensity of two immunoreactive bands of 39 and 43 kilodaltons that were detected with antibodies against CK-II. The chromatographic behaviour and immunoblotting data indicate that the phosvitin kinase peak represented CK-II and suggested that the rat spleen CK-II had a molecular structure of αα′β2. Furthermore, using an intact rat model, we showed that the potentially novel spleen MAP kinase and CK-II were markedly activated following intravenous injection of insulin. The significance of these findings remains to be determined.Key words: mitogen-activated protein kinase, S6 kinase, casein kinase II, insulin, spleen.

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48

Czernick, Drew, Jess Liu, Dibart Serge, and Erdjan Salih. "Topographical distribution of phosphorylation sites of phosvitins by mass spectrometry." Journal of Proteomics 83 (May 2013): 76–98. http://dx.doi.org/10.1016/j.jprot.2013.02.016.

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49

Jung, Samooel, Dong Uk Ahn, Ki Chang Nam, Hyun Joo Kim, and Cheorun Jo. "Separation of Phosvitin from Egg Yolk without Using Organic Solvents." Asian-Australasian Journal of Animal Sciences 26, no. 11 (November 1, 2013): 1622–29. http://dx.doi.org/10.5713/ajas.2013.13263.

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50

Jiang, Bo, and Yoshinori Mine. "Preparation of Novel Functional Oligophosphopeptides from Hen Egg Yolk Phosvitin." Journal of Agricultural and Food Chemistry 48, no. 4 (April 2000): 990–94. http://dx.doi.org/10.1021/jf990600l.

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