Isolation and characterization of beta- and gamma-caseins from horse milk.
Abstract: Three groups of casein components were isolated from horse milk. Group I is almost insoluble at acid and neutral pH, and is rather heterogeneous on alkaline gels with or without sodium dodecyl sulphate. Group II shows strong similarity to beta-casein from other species, as concluded from its amino acid composition and its N- and C-terminal sequences. This group consists of five electrophoretically distinguishable forms, all containing ester phosphate groups but no carbohydrate. Group III is composed of C-terminal fragments of the beta-like (group II) fraction and probably arises from the action of a plasmin-like enzyme present in horse milk. It does not contain phosphate or carbohydrate. Homology of this group with bovine gamma-caseins is demonstrated. Both beta- and gamma-like caseins are more soluble at 4 degrees C than at room temperature.
Publication Date: 1982-04-01 PubMed ID: 6213224PubMed Central: PMC1158202DOI: 10.1042/bj2030131Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This paper reveals that three casein components were isolated from horse milk, with each group having distinct characteristics and resemblances with similar forms found in other species.
Identification and Classification of Casein Components
- The paper explains that the casein components found in horse milk were classified into three groups due to their distinct natures and responses to various chemical environments.
- The first group (Group I) was one that showed high levels of insolubility when exposed to both acidic and neutral pH levels. Its behavior and structure were more heterogeneous, displaying varying forms when tested on alkaline gels in both the presence and absence of sodium dodecyl sulphate, a commonly used detergent for protein studies.
Characteristics of Beta-Casein Component
- Group II was found to have a strong similarity to beta-casein from other species. The observation was supported by the group’s amino acid composition and N- and C-terminal sequences features that define the basic structure of a protein.
- The researchers identified five different types within this group, all distinguished through electrophoretic methods.
- It was also noted that all forms in this group contained ester phosphate groups but no carbohydrate, adding to the chemical properties of this specific group.
Gamma-Casein and Its Origin
- The third group described (Group III) mainly consisted of C-terminal fragments of the beta-like casein (Group II). The researchers infer that this fraction arises due to the action of a plasmin-like enzyme which is present in horse milk.
- This group did not carry phosphate or carbohydrate contents.
- A similarity was drawn between this group and bovine gamma-caseins (gamma-casein found in cow milk), establishing its homology.
Solubility of Beta- and Gamma-like Caseins
- Lastly, it was observed that both beta- and gamma-like caseins were more soluble at a smaller temperature 4 degrees Celsius than at room temperature. This observation offers key insights into the behavior of these proteins in different temperature conditions which could have potential implications in milk processing and dairy products manufacturing.
Cite This Article
APA
Visser S, Jenness R, Mullin RJ.
(1982).
Isolation and characterization of beta- and gamma-caseins from horse milk.
Biochem J, 203(1), 131-139.
https://doi.org/10.1042/bj2030131 Publication
Researcher Affiliations
MeSH Terms
- Acid Phosphatase
- Amino Acid Sequence
- Amino Acids / analysis
- Animals
- Caseins / isolation & purification
- Cattle
- Chymosin
- Electrophoresis, Polyacrylamide Gel
- Electrophoresis, Starch Gel
- Female
- Fibrinolysin
- Horses
- Milk / analysis
- Molecular Weight
References
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Citations
This article has been cited 1 times.- Welsch U, Buchheim W, Schumacher U, Schinko I, Patton S. Structural, histochemical and biochemical observations on horse milk-fat-globule membranes and casein micelles. Histochemistry 1988;88(3-6):357-65.
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