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The Caseins of Milk as Calcium-Binding Proteins

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Calcium-Binding Protein Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 172))

Abstract

The virtual image of milk, which would be constructed by most people, is that of a creamy white fluid rich in calcium. The lubricity and taste of milk are related to this perception and are based upon three unique biological structures: the colloidal calcium-protein complexes (the casein micelles), the milk-fat globules with their limiting membrane, and the milk sugar:lactose (1). The complexity of these structures is necessitated by the fact that milk is, in essence, predominantly water. It is the accommodation of these ingredients to an aqueous environment that forms the basis for the structure of milk at the molecular level. Adaptation of milk components to their ultimate aqueous environment begins during secretion. Lipid and protein synthesis are partitioned from the start. Amino acids and their metabolic precursors are actively transported into the secretory epithelial cells and assembled into proteins on the ribosomes of the highly developed rough endoplasmic reticulum. All proteins of mammary origin have conserved leader sequences which cause insertion of the nascent proteins into the lumen of the endoplasmic reticulum (see Fig. 1). The proteins are then transported through the Golgi apparatus, as shown in Fig. 1; presumably the globular proteins of milk are folded during this period. In the Golgi apparatus, the caseins, which are the major milk proteins in most species, are phosphorylated to begin the process of calcium transport. In general, when milks that contain>2% protein are analyzed, the accompanying inorganic phosphate and calcium levels yield insoluble precipitates (apatite or brushite).

Cell physiology of lactating mammary gland. (A) A single alveolus consisting of lactating epithelial cells surrounding the lumen. (B) A typical lactating cell indicating active secretion of protein and lipid by distinct mechanisms. (Reprinted with permission from S. Patton, Sci. Am. July 1969).

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Authors and Affiliations

  1. Eastern Regional Research Center, United States Department of Agriculture, ARS, Wyndmoor, PA

    Harold M. Farrell Jr., Thomas F. Kumosinski, Edyth L. Malin & Eleanor M. Brown

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  1. Harold M. Farrell Jr.
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  2. Thomas F. Kumosinski
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  3. Edyth L. Malin
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  4. Eleanor M. Brown
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Editors and Affiliations

  1. Department of Biological Sciences, University of Calgary, Calgary, AB, Canada

    Hans J. Vogel

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© 2002 Humana Press Inc.

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Farrell, H.M., Kumosinski, T.F., Malin, E.L., Brown, E.M. (2002). The Caseins of Milk as Calcium-Binding Proteins. In: Vogel, H.J. (eds) Calcium-Binding Protein Protocols. Methods in Molecular Biology™, vol 172. Humana Press. https://doi.org/10.1385/1-59259-183-3:097

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  • DOI: https://doi.org/10.1385/1-59259-183-3:097

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-688-8

  • Online ISBN: 978-1-59259-183-1

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