Milk Proteins pp 112-123 | Cite as

Structure and Variability of Milk Proteins

  • B. Ribadeau-Dumas

Abstract

A protein molecule is best characterized when its tertiary structure has been elucidated by high resolution x-ray crystallography. As far as the main milk proteins are concerned, this was achieved in 1986 for two of them, baboon α-lactalbumin [1] and bovine β-lactoglobulin [2]. No one casein has ever been crystallized and, owing to their self-aggregation properties, it may be that these proteins will never be obtained in crystalline form. However, as for the other milk proteins, a great deal of information can be deduced from their primary structures. Indeed, for any biologically active protein, genetic variability does not usually affect the tertiary structure to a large extent even if the activity is strongly modified. A good example of this statement is the phylogenic relationship between α-lactalbumin and lysozyme that we shall discuss later on.

Keywords

Carbohydrate Cysteine Serine Proline Disulfide 

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Copyright information

© Dr. Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1989

Authors and Affiliations

  • B. Ribadeau-Dumas
    • 1
  1. 1.Dairy Research LaboratoryInstitut National de la Recherche AgronomiqueJouy-en-JosasFrance

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