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Amino Acid Composition of γ-Casein

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    Amino Acid Composition of γ-Casein
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 1953, 75, 7, 1678–1679
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    https://doi.org/10.1021/ja01103a048
    Published April 1, 1953
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    This article is cited by 26 publications.

    1. Ruijie Zhang, Fangfang Su, Yi Zhang. Hollow capsules formed by the self-assembly of caseins on sessile air bubbles. Colloids and Surfaces A: Physicochemical and Engineering Aspects 2011, 375 (1-3) , 124-129. https://doi.org/10.1016/j.colsurfa.2010.11.072
    2. M. Khristov, G. Gyurov, P. Peshev. Preparation of rhenium disilicide crystals. Crystal Research and Technology 1989, 24 (2) https://doi.org/10.1002/crat.2170240223
    3. M. Kirchgessner, Brigitte R. Paulicks. Aminosäuren in der Kuhmilch während und nach energetischer Überversorgung. Journal of Animal Physiology and Animal Nutrition 1988, 60 (1-5) , 229-233. https://doi.org/10.1111/j.1439-0396.1988.tb00196.x
    4. M. Kirchgessner, M. Kreuzer. Aminosäurenmuster des Milchproteins während und nach Über‐ oder Unterversorgung der Kuh mit Rohprotein. Journal of Animal Physiology and Animal Nutrition 1988, 59 (1-5) , 150-159. https://doi.org/10.1111/j.1439-0396.1988.tb00058.x
    5. Frank A. Lee. Milk and Milk Products. 1983, 363-395. https://doi.org/10.1007/978-94-011-7376-6_16
    6. J.L. Jorda, M. Ishikawa, J. Muller. Phase relations and superconductivity in the binary Re-Si system. Journal of the Less Common Metals 1982, 85 , 27-35. https://doi.org/10.1016/0022-5088(82)90055-8
    7. Luciano Cecchi, Pierpaolo Resmini, Mario Pace. Ein möglicher Mechanismus zur Bildung vonα-Aminobuttersäure während der Käsereifung. Zeitschrift für Lebensmittel-Untersuchung und -Forschung 1974, 156 (2) , 81-86. https://doi.org/10.1007/BF02425626
    8. R.G. Derrig, J.H. Clark, C.L. Davis. Effect of Abomasal Infusion of Sodium Caseinate on Milk Yield, Nitrogen Utilization and Amino Acid Nutrition of the Dairy Cow. The Journal of Nutrition 1974, 104 (2) , 151-159. https://doi.org/10.1093/jn/104.2.151
    9. Dyson Rose, J.R. Brunner, E.B. Kalan, B.L. Larson, P. Melnychyn, H.E. Swaisgood, D.F. Waugh. Nomenclature of the Proteins of Cow's Milk: Third Revision. Journal of Dairy Science 1970, 53 (1) , 1-17. https://doi.org/10.3168/jds.S0022-0302(70)86141-0
    10. M.L. Groves, W.G. Gordon. Evidence from amino acid analysis for a relationship in the biosynthesis of γ- and β-caseins. Biochimica et Biophysica Acta (BBA) - Protein Structure 1969, 194 (2) , 421-432. https://doi.org/10.1016/0005-2795(69)90102-0
    11. M.L. Groves. Some Minor Components of Casein and Other Phosphoproteins in Milk. A Review. Journal of Dairy Science 1969, 52 (8) , 1155-1165. https://doi.org/10.3168/jds.S0022-0302(69)86718-4
    12. Kamala K. Tripathi, Charles W. Gehrke. Chromatography and characterization of γ-casein. Journal of Chromatography A 1969, 43 , 322-331. https://doi.org/10.1016/S0021-9673(00)99208-2
    13. Jean Leclercq, Luis Lopez-Francos. Nutrition Protidique Chez Tenebrio Molitor L . VIII. — Sur La Valeur Nutritive Des Fractions De La Caséine. Archives Internationales de Physiologie et de Biochimie 1967, 75 (1) , 89-95. https://doi.org/10.3109/13813456709084922
    14. P. Jollègs. Fortschritte auf dem Gebiet der Casein‐Chemie. Angewandte Chemie 1966, 78 (12) , 629-637. https://doi.org/10.1002/ange.19660781203
    15. P. Jollès. Progress in the Chemistry of Casein. Angewandte Chemie International Edition in English 1966, 5 (6) , 558-566. https://doi.org/10.1002/anie.196605581
    16. Joseph S. Chen, Wen‐Kuo Ting. Isolation and Amino Acid Composition of Human Milk Casein and its Components. Journal of the Chinese Chemical Society 1966, 13 (1) , 1-12. https://doi.org/10.1002/jccs.196600001
    17. R. Beutler. Vergleichende Physiologische Chemie. 1966, 659-970. https://doi.org/10.1007/978-3-662-37018-6_2
    18. H.U. Bohren, V.R. Wenner. Natural State of Milk Proteins. I. Composition of the Micellar and Soluble Casein of Milk After Ultracentrifugal Sedimentation. Journal of Dairy Science 1961, 44 (7) , 1213-1223. https://doi.org/10.3168/jds.S0022-0302(61)89872-X
    19. William G. Gordon, Jay J. Basch. Tryptophan content of purified milk proteins. Biochimica et Biophysica Acta 1961, 48 (2) , 397-398. https://doi.org/10.1016/0006-3002(61)90491-7
    20. E.R. LING, S.K. KON, J.W.G. PORTER. The Composition of Milk and the Nutritive Value of its Components. 1961, 195-263. https://doi.org/10.1016/B978-1-4832-3225-6.50009-0
    21. Gerhard Schmidt. Phosphoproteide. 1960, 618-661. https://doi.org/10.1007/978-3-642-85729-4_7
    22. G.K. Murthy, R.McL. Whitney. A Comparison of Some of the Chemical and Physical Properties of γ-Casein and Immune Globulins of Milk. Journal of Dairy Science 1958, 41 (1) , 1-12. https://doi.org/10.3168/jds.S0022-0302(58)90860-9
    23. R.G. Hansen, D.M. Carlson. An Evaluation of the Balance of Nutrients in Milk. Journal of Dairy Science 1956, 39 (6) , 663-673. https://doi.org/10.3168/jds.S0022-0302(56)91187-0
    24. R. Aschaffenburg. Section C. Dairy Chemistry: Part I. Milk proteins and enzymes. Journal of Dairy Research 1956, 23 (1) , 134-143. https://doi.org/10.1017/S0022029900008128
    25. Royal A. Sullivan, Margaret M. Fitzpatrick, Elizabeth K. Stanton, Raymond Annino, George Kissel, Frank Palermiti. The influence of temperature and electrolytes upon the apparent size and shape of α- and β-casein. Archives of Biochemistry and Biophysics 1955, 55 (2) , 455-468. https://doi.org/10.1016/0003-9861(55)90426-4
    26. S. K. Kon, K. M. Henry. Section D. Nutritive value of milk and milk products. Journal of Dairy Research 1954, 21 (2) , 245-298. https://doi.org/10.1017/S0022029900007342
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    Journal of the American Chemical Society

    Cite this: J. Am. Chem. Soc. 1953, 75, 7, 1678–1679
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ja01103a048
    Published April 1, 1953
    Request reuse permissions

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