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Journal of Dairy Science Vol. 67 No. 8 1599-1631
© 1984 by American Dairy Science Association ®
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Nomenclature of Proteins of Cow's Milk: Fifth Revision1

W. N. Eigel, Chairman

Department of Food Science and Technology, Virginia Polytechnic Institute and State University, Blacksburg 24061

J. E. Butler

Department of Microbiology, College of Medicine, University of Iowa, Iowa City 52240

C. A. Ernstrom

Department of Food Science, Utah State University, Logan 84321

H. M. Farrell, Jr.

Eastern Regional Research Center, Agricultural Research Service, US Department of Agriculture, Philadelphia 19118

V. R. Harwalkar

Food Research Institute, Agriculture Canada, Ottawa, Canada

R. Jenness

Department of Biochemistry, University of Minnesota, St. Paul 55108

R. McL. Whitney

Department of Food Science, University of Illinois, Urbana 61801

ABSTRACT

This report reviews changes the nomenclature of bovine milk proteins necessitated by recent advances of our knowledge. Identification of a number of milk proteins ({alpha}s1-, ß-, and {kappa}-caseins; {alpha}-lactalbumin and ß-lactoglobulin) continues to be based upon their primary structures (amino acid sequences). Since our last report, {alpha}s2-casein and serum albumin can be added to the list of major milk proteins for primary structure is known. Changes recommended in the nomenclature of caseins are primarily a result of differences within this family of proteins brought about by posttranslational modification. For example, {alpha}s0-casein is identical to {alpha}s1-casein, and {alpha}s3-, {alpha}s4-, and {alpha}s6-caseins are identical to {alpha}s2-casein except for differences in degree of phosphorylation. Additionally, proteose-peptone components 5, 8-slow and 8-fast, and {gamma}1-, {gamma}2-, and {gamma}3-caseins are N-terminal and C-terminal fragments, respectively, of ß-casein formed during proteolysis by plasmin. Nomenclature of immunoglobulins remains consistent with guidelines for human proteins and is based largely upon crossreactivity with reference proteins.

The minor whey protein lactollin is ß2-microglobulin for which the sequence of amino acids is known. An operational definition for proteins associated with the milk fat globule membrane has been developed. Nomenclature initially suggested for these proteins was based upon their electrophoretic behavior under a given set of conditions.

Because of increased interest in milk proteins of species other than bovine, the Committee suggests that these be identified as homologs of those already characterized in European, Bos taurus, and Indian, Bos indicus, cattle. Guidelines are given to aid in determining if homology exists. Provisional nomenclature is suggested for use in the interim until homology can be established.


FOOTNOTES

1 Report of the Committee on the Nomenclature and Methodology of Milk Proteins of the Dairy Foods Research Section, Dairy Foods Division, American Dairy Science Association.




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