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An Electrophoretic Study of the Proteins of Egg White

Cite this: J. Am. Chem. Soc. 1940, 62, 10, 2580–2590
Publication Date (Print):October 1, 1940
https://doi.org/10.1021/ja01867a002
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    2. Begoña Monterroso, Belén Reija, Mercedes Jiménez, Silvia Zorrilla, Germán Rivas, . Charged Molecules Modulate the Volume Exclusion Effects Exerted by Crowders on FtsZ Polymerization. PLOS ONE 2016, 11 (2) , e0149060. https://doi.org/10.1371/journal.pone.0149060
    3. Yoshinori Mine. Egg Proteins. 2014, 459-490. https://doi.org/10.1002/9781118860588.ch17
    4. Natasha Whenham, Peter W. Wilson, Maureen M. Bain, Lynn Stevenson, Ian C. Dunn. Comparative biology and expression of TENP, an egg protein related to the bacterial permeability-increasing family of proteins. Gene 2014, 538 (1) , 99-108. https://doi.org/10.1016/j.gene.2013.12.065
    5. M. Tixier-Boichard, F. Leenstra, D.K Flock, P.M. Hocking, S. Weigend. A century of poultry genetics. World's Poultry Science Journal 2012, 68 (2) , 307-321. https://doi.org/10.1017/S0043933912000360
    6. Yukiko Murakami, Ken Sugo, Masahiro Hirano, Tsuneo Okuyama. Improved Preparation Method of Polyethylenimine-Hydroxyapatite and Its Chromatographic Properties. Separation Science and Technology 2011, 46 (8) , 1306-1312. https://doi.org/10.1080/01496395.2011.554950
    7. Yoshinori Mine, Marie Yang. Functional Properties of Egg Components in Food Systems. 2010, 579-630. https://doi.org/10.1002/9780470504451.ch29
    8. Myung-Suk Chun, Intaek Lee. Rigorous estimation of effective protein charge from experimental electrophoretic mobilities for proteomics analysis using microchip electrophoresis. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2008, 318 (1-3) , 191-198. https://doi.org/10.1016/j.colsurfa.2007.12.046
    9. Valerie Lechevalier, Thomas Croguennec, Françoise Nau, Catherine Guérin-Dubiard. Ovalbumin and Gene-Related Proteins. 2007, 51-60. https://doi.org/10.1007/978-3-540-37885-3_8
    10. E Charter, J Losso, S Nakai. Lysozyme. 2000https://doi.org/10.1201/9781420039368.ch6
    11. Yoshinori Mine. Recent advances in the understanding of egg white protein functionality. Trends in Food Science & Technology 1995, 6 (7) , 225-232. https://doi.org/10.1016/S0924-2244(00)89083-4
    12. N.G. Douglas, A.A. Humffray, H.R.C. Pratt, G.W. Stevens. Electrophoretic mobilities of proteins and protein mixtures. Chemical Engineering Science 1995, 50 (5) , 743-754. https://doi.org/10.1016/0009-2509(94)00434-S
    13. A.C. Awadé, S. Moreau, D. Mollé, G. Brulé, J.-L. Maubois. Two-step chromatographic procedure for the purification of hen egg white ovomucin, lysozyme, ovotransferrin and ovalbumin and characterization of purified proteins. Journal of Chromatography A 1994, 677 (2) , 279-288. https://doi.org/10.1016/0021-9673(94)80156-8
    14. Lewis Stevens. Egg white proteins. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 1991, 100 (1) , 1-9. https://doi.org/10.1016/0305-0491(91)90076-P
    15. L. Stevens, D. Duncan. Peptide mapping of ovoglobulins G2A and G2B in the domestic fowl. British Poultry Science 1988, 29 (3) , 665-669. https://doi.org/10.1080/00071668808417092
    16. William D. Powrie, S. Nakai. The Chemistry of Eggs and Egg Products. 1986, 97-139. https://doi.org/10.1007/978-1-349-09142-3_6
    17. R. D. GALYEAN, J. A. LANEY. SODIUM DODECYL SULFATE‐POLYACRYLAMIDE GEL ELECTROPHORESIS OF, CHROMATOGRAPHICALLY FRACTIONATED EGG WHITE. Journal of Food Science 1980, 45 (3) , 460-462. https://doi.org/10.1111/j.1365-2621.1980.tb04075.x
    18. Takatoshi Itoh, Hiroshi Sugawara, Susumu Adachi. Isolation and characterization of new minor proteins (Ovoglycocomponents) from chicken and quail egg whites. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 1980, 67 (2) , 261-264. https://doi.org/10.1016/0305-0491(80)90142-X
    19. R. D. GALYEAN, O. J. COTTERILL. CHROMATOGRAPHY AND ELECTROPHORESIS OF NATIVE AND SPRAY‐DRIED EGG WHITE. Journal of Food Science 1979, 44 (5) , 1345-1349. https://doi.org/10.1111/j.1365-2621.1979.tb06435.x
    20. S.K. Gayen, S. Som, N.K. Sinha, A. Sen. Lysozyme in egg whites of tortoises and turtle. Archives of Biochemistry and Biophysics 1977, 183 (2) , 432-442. https://doi.org/10.1016/0003-9861(77)90378-2
    21. VIRGINIA SHEPHERD, REX MONTGOMERY. Ovalbumin of Chicken Egg White. 1976, 172-174. https://doi.org/10.1016/B978-0-12-746207-3.50037-1
    22. Henry Ng, John A. Garibaldi. Death of Staphylococcus aureus in Liquid Whole Egg Near pH 8. Applied Microbiology 1975, 29 (6) , 782-786. https://doi.org/10.1128/am.29.6.782-786.1975
    23. John W. Donovan, Carol J. Mapes, John Gorton Davis, John A. Garibaldi. A differential scanning calorimetric study of the stability of egg white to heat denaturation. Journal of the Science of Food and Agriculture 1975, 26 (1) , 73-83. https://doi.org/10.1002/jsfa.2740260109
    24. David T. Osuga, Robert E. Feeney. AVIAN EGG WHITES. 1974, 39-71. https://doi.org/10.1016/B978-0-12-449940-9.50007-6
    25. . Lysozyme Bibliography: 1922–1972. 1974, 493-621. https://doi.org/10.1016/B978-0-12-528950-4.50050-2
    26. George Taborsky. Phosphoproteins. 1974, 1-210. https://doi.org/10.1016/S0065-3233(08)60230-2
    27. D. V. Vadehra, K. R. Nath, Richard Forsythe. Eggs as a source of protein. C R C Critical Reviews in Food Technology 1973, 4 (2) , 193-309. https://doi.org/10.1080/10408397309527158
    28. R. L. Munier, A. M. Drapier, B. Faivre. Nouveaux échangeurs d'ions hydrophiles pour la chromatographie des protéines: Pipéridine-N-éthyl-cellulose et Di-isopropyl-aminoéthyl-cellulose. Chromatographia 1973, 6 (7) , 305-313. https://doi.org/10.1007/BF02269331
    29. P. CHANG, W. D. POWRIE, O. FENNEMA. DISC GEL ELECTROPHORESIS OF PROTEINS IN NATIVE AND HEAT‐TREATED ALBUMEN, YOLK, AND CENTRIFUGED WHOLE EGG. Journal of Food Science 1970, 35 (6) , 774-778. https://doi.org/10.1111/j.1365-2621.1970.tb01992.x
    30. R.A. Mills. Analysis of electrophoretic boundary gradient patterns. Archives of Biochemistry and Biophysics 1970, 140 (2) , 425-429. https://doi.org/10.1016/0003-9861(70)90084-6
    31. Cheng-Chun Huang, Howard E. Mayer, Rex Montgomery. Microheterogeneity and paucidispersity of glycoproteins. Carbohydrate Research 1970, 13 (1) , 127-137. https://doi.org/10.1016/S0008-6215(00)84902-2
    32. U. Freimuth, W. Krause, B. Meisegeier. Nachweis von Fremdproteinen in Fleischerzeugnissen 1. Mitt. Nachweis von Eiklar in Brühwürsten mittels Elektrophorese in Polyacrylamidgel. Food / Nahrung 1970, 14 (1) , 13-18. https://doi.org/10.1002/food.19700140104
    33. Beatrice Kassell. [66g] Proteinase inhibitors from egg white. 1970, 890-906. https://doi.org/10.1016/0076-6879(70)19079-3
    34. R.G. Board. The Microbiology of the Hen's Egg. 1970, 245-281. https://doi.org/10.1016/S0065-2164(08)70612-9
    35. C.M. Ann Baker, G. Croizier, A. Strati, C. Manwell. Identity and Nomenclature of Some Protein Polymorphisms of Chicken Eggs and Sera. 1970, 147-174. https://doi.org/10.1016/S0065-2660(08)60073-5
    36. R. E. Feeney, St. K. Komatsu. The transferrins. , 149-206. https://doi.org/10.1007/BFb0119551
    37. JÖRGEN BÄCKSTRÖM. Distribution Studies of Mercuric Pesticides in Quail and Some Fresh‐Water Fishes. Acta Pharmacologica et Toxicologica 1969, 27 (S3) , 1-113. https://doi.org/10.1111/j.1600-0773.1969.tb03070.x
    38. S. I. Ankier. Reactivity of Rat and Man to Egg-White. 1969, 340-394. https://doi.org/10.1007/978-3-0348-7068-9_7
    39. C.M. Ann Baker, Clyde Manwell. Molecular genetics of avian proteins—VIII. Egg white proteins of the migratory quail, coturnix coturnix—New concepts of “hybrid vigour”. Comparative Biochemistry and Physiology 1967, 23 (1) , 21-42. https://doi.org/10.1016/0010-406X(67)90470-7
    40. A. Stratil. The effect of iron addition to avian egg white on the behaviour of conalbumin fractions in starch gel electrophoresis. Comparative Biochemistry and Physiology 1967, 22 (1) , 227-233. https://doi.org/10.1016/0010-406X(67)90183-1
    41. T. L. Parkinson. Effect of pasteurisation on the chemical composition of liquid whole egg. I.—Development of a scheme for the fractionation of the proteins of whole egg. Journal of the Science of Food and Agriculture 1967, 18 (5) , 208-213. https://doi.org/10.1002/jsfa.2740180509
    42. C.M.Ann Baker. Molecular genetics of avian proteins-VII. Chemical and genetic polymorphism of conalbumin and transferrin in a number of species. Comparative Biochemistry and Physiology 1967, 20 (3) , 949-973. https://doi.org/10.1016/0010-406X(67)90066-7
    43. . Antigens. 1967, 1-196. https://doi.org/10.1016/B978-0-12-754401-4.50007-5
    44. Yoshio Tomimatsu, John J. Clary, John J. Bartulovich. Physical characterization of ovoinhibitor, a trypsin and chymotrypsin inhibitor from chicken egg white. Archives of Biochemistry and Biophysics 1966, 115 (3) , 536-544. https://doi.org/10.1016/0003-9861(66)90073-7
    45. Shojiro Nakamura, Minoru Nagao, Ryosuke Suzono. Distribution of trypsin inhibitors in the egg white proteins of various birds. Comparative Biochemistry and Physiology 1966, 18 (4) , 937-IN27. https://doi.org/10.1016/0010-406X(66)90224-6
    46. R. G. BOARD. The Course of Microbial Infection of the Hen's Egg. Journal of Applied Bacteriology 1966, 29 (2) , 319-341. https://doi.org/10.1111/j.1365-2672.1966.tb03482.x
    47. T. L. Parkinson. The chemical composition of eggs. Journal of the Science of Food and Agriculture 1966, 17 (3) , 101-111. https://doi.org/10.1002/jsfa.2740170301
    48. C.M.Ann Baker, Clyde Manwell, Ronald F. Labisky, James A. Harper. Molecular genetics of avian proteins—V. Egg, blood and tissue proteins of the ring-necked pheasant, Phasianus colchicus L.. Comparative Biochemistry and Physiology 1966, 17 (2) , 467-499. https://doi.org/10.1016/0010-406X(66)90581-0
    49. ALFRED GOTTSCHALK, E.R. BRUCE GRAHAM. The Basic Structure of Glycoproteins. 1966, 95-151. https://doi.org/10.1016/B978-0-12-395726-9.50012-7
    50. C.M Ann Baker. Molecular genetics of avian proteins—III. The egg proteins of an isolated population of jungle fowl, Gallus Gallus L.. Comparative Biochemistry and Physiology 1964, 12 (3) , 389-403. https://doi.org/10.1016/0010-406X(64)90067-2
    51. I. E. Lush. Egg albumen polymorphisms in the fowl: The ovalbumin locus. Genetical Research 1964, 5 (2) , 257-268. https://doi.org/10.1017/S001667230000121X
    52. F.E. Cunningham, O.J. Cotterill. Factors Affecting Acid Coagulation of the Egg White. Poultry Science 1964, 43 (1) , 53-59. https://doi.org/10.3382/ps.0430053
    53. Kunio Matsui, Kei Yaeno. Quantitative starch gel electrophoresis. Analytical Biochemistry 1963, 6 (6) , 491-503. https://doi.org/10.1016/0003-2697(63)90142-8
    54. Joan R. Clark, David T. Osuga, Robert E. Feeney. Comparison of Avian Egg White Conalbumins. Journal of Biological Chemistry 1963, 238 (11) , 3621-3631. https://doi.org/10.1016/S0021-9258(19)75317-4
    55. W. CAREY PARKER, ALEXANDER G. BEARN. Boric Acid-induced Heterogeneity of Conalbumin by Starch-gel Electrophoresis. Nature 1963, 199 (4899) , 1184-1186. https://doi.org/10.1038/1991184b0
    56. Robert E. Feeney, Hans Abplanalp, John J. Clary, David L. Edwards, Joan R. Clark. A Genetically Varying Minor Protein Constituent of Chicken Egg White. Journal of Biological Chemistry 1963, 238 (5) , 1732-1736. https://doi.org/10.1016/S0021-9258(18)81128-0
    57. W.E. Seideman, O.J. Cotterill, E.M. Funk. Factors Affecting Heat Coagulation of Egg White. Poultry Science 1963, 42 (2) , 406-417. https://doi.org/10.3382/ps.0420406
    58. A.N. Glazer, H.A. McKenzie. The denaturation of proteins IV. Conalbumin and iron(III)-conalbumin in urea soloution. Biochimica et Biophysica Acta 1963, 71 , 109-123. https://doi.org/10.1016/0006-3002(63)90990-9
    59. Delma Cochrane, E. Annau. ELECTROPHORETIC DIFFERENCES IN THE EGG-WHITE PROTEINS OF THE HEN. Canadian Journal of Biochemistry and Physiology 1962, 40 (10) , 1335-1341. https://doi.org/10.1139/o62-148
    60. C. M. Ann Baker, Clyde Manwell. Molecular genetics of avian proteins. British Poultry Science 1962, 3 (3) , 161-174. https://doi.org/10.1080/00071666208415471
    61. E. ANNAU, DELMA COCHRANE. Comparative Starch-gel Electrophoretic Studies of Fowl Egg White and Plasma. Nature 1962, 193 (4818) , 879-880. https://doi.org/10.1038/193879a0
    62. Delma Cochrane, E. Annau. ELECTROPHORETIC DIFFERENCES IN THE EGG-WHITE PROTEINS OF THE HEN. Canadian Journal of Biochemistry and Physiology 1962, 40 (1) , 1335-1341. https://doi.org/10.1139/y62-148
    63. Robert E. Feeney, Robert M. Hill. Protein Chemistry and Food Research. 1961, 23-73. https://doi.org/10.1016/S0065-2628(08)60135-4
    64. CHARLES G. SIBLEY. THE ELECTROPHORETIC PATTERNS OF AVIAN EGG‐WHITE PROTEINS AS TAXONOMIC CHARACTERS*. Ibis 1960, 102 (2) , 215-284. https://doi.org/10.1111/j.1474-919X.1960.tb07114.x
    65. H.-J. Bielig, E. Bayer. Metallproteide und verwandte Systeme. 1960, 714-773. https://doi.org/10.1007/978-3-642-85729-4_9
    66. F.R. Jevons. The heterogeneity of ovomucoid. Biochimica et Biophysica Acta 1960, 45 , 384-386. https://doi.org/10.1016/0006-3002(60)91465-7
    67. Stanley Mandeles. Use of DEAE-cellulose in the separation of proteins from egg white and other biological materials. Journal of Chromatography A 1960, 3 , 256-264. https://doi.org/10.1016/S0021-9673(01)96990-0
    68. . Sedimentation and electrophoresis of interacting substances, II. Asymptotic boundary shape for two substances interacting reversibly. Proceedings of the Royal Society of London. Series A. Mathematical and Physical Sciences 1959, 420-437. https://doi.org/10.1098/rspa.1959.0204
    69. J.M. Katyal, George Gorin. Determination of mercapto groups in ovalbumin with ferricyanide. Archives of Biochemistry and Biophysics 1959, 82 (2) , 319-329. https://doi.org/10.1016/0003-9861(59)90127-4
    70. Kin'ichi Matsushima. An Undescribed Trypsin Inhibitor in Egg White. Science 1958, 127 (3307) , 1178-1179. https://doi.org/10.1126/science.127.3307.1178
    71. Lars Odin. Mucopolysaccharides of Epithelial Mucus. 1958, 234-244. https://doi.org/10.1002/9780470719060.ch14
    72. Marvin B. Rhodes, Parviz R. Azari, Robert E. Feeney. ANALYSIS, FRACTIONATION, AND PURIFICATION OF EGG WHITE PROTEINS WITH CELLULOSE-CATION EXCHANGER. Journal of Biological Chemistry 1958, 230 (1) , 399-408. https://doi.org/10.1016/S0021-9258(18)70575-9
    73. John R. Cann, Robert A. Phelps. On the modification of conalbumin by acid. Biochimica et Biophysica Acta 1957, 26 (2) , 378-386. https://doi.org/10.1016/0006-3002(57)90020-3
    74. ROY L. WHISTLER, W.M. CORBETT. POLYSACCHARIDES (1). 1957, 641-732. https://doi.org/10.1016/B978-0-12-395709-2.50016-6
    75. MARIE KAMINSKI. Globulins in the Chicken Egg-White. Nature 1956, 178 (4540) , 981-982. https://doi.org/10.1038/178981b0
    76. Robert A. Phelps, John R. Cann. On the modification of conalbumin by acid. II. Effect of pH and salt concentration on the sedimentation behavior, viscosity and osmotic pressure of conalbumin solutions. Archives of Biochemistry and Biophysics 1956, 61 (1) , 51-71. https://doi.org/10.1016/0003-9861(56)90316-2
    77. J.M. Gonçalves, R. Molinari, H.F. Deutsch. Chromatographic and immunochemical studies on lysozyme. Archives of Biochemistry and Biophysics 1956, 60 (1) , 171-179. https://doi.org/10.1016/0003-9861(56)90409-X
    78. Emil L. Smith, J.R. Kimmel, Douglas M. Brown, E. O.P. Thompson. ISOLATION AND PROPERTIES OF A CRYSTALLINE MERCURY DERIVATIVE OF A LYSOZYME FROM PAPAYA LATEX. Journal of Biological Chemistry 1955, 215 (1) , 67-89. https://doi.org/10.1016/S0021-9258(18)66018-1
    79. John R. Cann, Robert A. Phelps. On the modification of conalbumin by acid. I. Electrophoretic and sedimentation studies on conalbumin prepared by ammonium sulfate precipitation from acid solutions. Archives of Biochemistry and Biophysics 1954, 52 (1) , 48-65. https://doi.org/10.1016/0003-9861(54)90088-0
    80. Patrio Caselli, Heinz Schumacher. Mikro-elektrophoretische Studien mit dem Serum-Lysozym. Zeitschrift für Die Gesamte Experimentelle Medizin 1954, 124 (1) , 65-71. https://doi.org/10.1007/BF02045869
    81. H.F. Deutsch. FETUIN: THE MUCOPROTEIN OF FETAL CALF SERUM. Journal of Biological Chemistry 1954, 208 (2) , 669-678. https://doi.org/10.1016/S0021-9258(18)65593-0
    82. Emil L. Smith, J.R. Kimmel, Douglas M. Brown. CRYSTALLINE PAPAIN. Journal of Biological Chemistry 1954, 207 (2) , 533-549. https://doi.org/10.1016/S0021-9258(18)65670-4
    83. N. MICHAEL GREEN, HANS NEURATH. Proteolytic Enzymes. 1954, 1057-1198. https://doi.org/10.1016/B978-0-12-395721-4.50011-1
    84. ROBERT C. WARNER. Egg Proteins. 1954, 435-485. https://doi.org/10.1016/B978-0-12-395722-1.50010-0
    85. M. Laskowski, M. Laskowski. Naturally Occurring Trypsin Inhibitors. 1954, 203-242. https://doi.org/10.1016/S0065-3233(08)60207-7
    86. M. Bier, L. Terminiello, Joseph A. Duke, Robert J. Gibbs, F.F. Nord. Investigations on proteins and polymers. X. Composition and fractionation of ovomucoid. Archives of Biochemistry and Biophysics 1953, 47 (2) , 465-473. https://doi.org/10.1016/0003-9861(53)90483-4
    87. H. Deuel, J. Solms, A. Denzler. Flockungsreaktionen zwischen polymeren Säuren und polymeren Basen. Helvetica Chimica Acta 1953, 36 (6) , 1671-1680. https://doi.org/10.1002/hlca.19530360655
    88. Luigi Gorini, Lucienne Audrain. Le complexe ovomocoïde-trypsine. Son activité protéolytique et le rôle de quelques métaux dans la stabilité de ses constituants. Biochimica et Biophysica Acta 1953, 10 , 570-579. https://doi.org/10.1016/0006-3002(53)90299-6
    89. Sherman R. Dickman, Charles M. Proctor. Factors affecting the activity of egg white lysozyme. Archives of Biochemistry and Biophysics 1952, 40 (2) , 364-372. https://doi.org/10.1016/0003-9861(52)90124-0
    90. Hans. Hoch, Alfred. Chanutin. EFFECTS OF ANTICOAGULANTS ON SERUM AND PLASMA. Journal of Biological Chemistry 1952, 197 (2) , 503-511. https://doi.org/10.1016/S0021-9258(18)55605-2
    91. M. Bier, Joseph A. Duke, Robert J. Gibbs, F.F. Nord. Composition and fractionation of ovomucoid. Archives of Biochemistry and Biophysics 1952, 37 (2) , 491-493. https://doi.org/10.1016/0003-9861(52)90211-7
    92. Frank A. Csonka, Merriam A. Jones. Factors Affecting the Percentage of Certain Proteins in Egg White. The Journal of Nutrition 1952, 46 (4) , 531-537. https://doi.org/10.1093/jn/46.4.531
    93. L.R. Wetter, H.F. Deutsch. IMMUNOLOGICAL STUDIES ON EGG WHITE PROTEINS. Journal of Biological Chemistry 1951, 192 (1) , 237-242. https://doi.org/10.1016/S0021-9258(18)55926-3
    94. L.R. MacDonnell, R.B. Silva, R.E. Feeney. The sulfhydryl groups of ovalbumin. Archives of Biochemistry and Biophysics 1951, 32 (2) , 288-299. https://doi.org/10.1016/0003-9861(51)90274-3
    95. Robert C. Warner, Ione Weber. THE PREPARATION OF CRYSTALLINE CONALBUMIN. Journal of Biological Chemistry 1951, 191 (1) , 173-180. https://doi.org/10.1016/S0021-9258(18)50964-9
    96. Howard. Tint, Wilhelm. Reiss. SOME PROPERTIES OF A BACILLOMYCIN b-CYTOCHROME c COMPLEX. Journal of Biological Chemistry 1951, 190 (1) , 133-148. https://doi.org/10.1016/S0021-9258(18)56054-3
    97. Richard H. Forsythe, Joseph F. Foster. EGG WHITE PROTEINS. Journal of Biological Chemistry 1950, 184 (1) , 377-383. https://doi.org/10.1016/S0021-9258(19)51158-9
    98. Richard H. Forsythe, Joseph F. Foster. EGG WHITE PROTEINS. Journal of Biological Chemistry 1950, 184 (1) , 385-392. https://doi.org/10.1016/S0021-9258(19)51159-0
    99. D.P. Riley, D. Herbert. Molecular size, shape and aggregation in concentrated protein solutions as revealed by X-ray scattering Haemoglobin and egg-albumin. Biochimica et Biophysica Acta 1950, 4 , 374-384. https://doi.org/10.1016/0006-3002(50)90043-6
    100. J.R. Hawthorne. The action of egg white lysozyme on ovomucoid and ovomucin. Biochimica et Biophysica Acta 1950, 6 , 28-35. https://doi.org/10.1016/0006-3002(50)90074-6
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