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Journal of dairy science1976; 59(5); 816-822; doi: 10.3168/jds.S0022-0302(76)84281-6

Isolation of kappa-casein-like proteins from milks of various species.

Abstract: Kappa-Casein-like proteins were isolated from the milks of cow, goat, reindeer, horse, rat, and rabbit. When treated with rennin, all of the isolated kappa-casein components yielded para-kappa-casein-like bands on gel electrophoresis. The rate of cleavage of these components with rennin was determined by measuring material soluble in trichloroacetic acid (macropeptide). The curves were characteristic of a limited, specific attack by rennin on these proteins. The goat and reindeer kappa-caseins were nearly as bovine kappa-casein, but the cleavage of horse, rat, and rabbit kappa-casein-like components was much slower.
Publication Date: 1976-05-01 PubMed ID: 773973DOI: 10.3168/jds.S0022-0302(76)84281-6Google Scholar: Lookup
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  • Journal Article

Summary

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The research article is about the isolation of kappa-casein-like proteins from various species including cow, goat, reindeer, horse, rat, and rabbit.

Isolation of kappa-casein-like proteins

  • The study involves the isolation of kappa-casein-like proteins from the milk of various species, namely cow, goat, reindeer, horse, rat, and rabbit.
  • The presence of kappa-casein-like proteins in all these species indicates that it could be a common component in mammalian milk.

Treatment with Rennin

  • After isolation, the kappa-casein components from each species were then treated with rennin, an enzyme that cleaves certain proteins.
  • The resulting products were then observed on a gel electrophoresis, a method used to separate proteins based on size and charge.
  • All treated kappa-casein proteins yielded para-kappa-casein-like bands, implying that rennin triggers a certain cleavage reaction in these proteins resulting in similar fragments, regardless of the species.

Determination of Cleavage Rate

  • The rate of cleavage of these kappa-casein components by rennin was assessed, which provides information about how quickly the protein can be broken down by the enzyme. This was measured by determining the soluble material in trichloroacetic acid, a procedure known as macropeptide analysis.
  • The results displayed curves that were characteristic of a limited, specific attack by rennin, suggesting that this enzyme consciously targets these proteins and doesn’t fully disassemble them.
  • The kappa-caseins from goat and reindeer were cleaved nearly as quickly as those from bovine. However, the kappa-caseins from horse, rat, and rabbit were cleaved significantly slower.

Implications

  • The results of this research could be significant in understanding the different digestion rates in different mammals and also aid in the development of dairy products tailored for various species.

Cite This Article

APA
Kotts C, Jenness R. (1976). Isolation of kappa-casein-like proteins from milks of various species. J Dairy Sci, 59(5), 816-822. https://doi.org/10.3168/jds.S0022-0302(76)84281-6

Publication

ISSN: 0022-0302
NlmUniqueID: 2985126R
Country: United States
Language: English
Volume: 59
Issue: 5
Pages: 816-822

Researcher Affiliations

Kotts, C
    Jenness, R

      MeSH Terms

      • Animals
      • Caseins / isolation & purification
      • Caseins / metabolism
      • Cattle
      • Chymosin / metabolism
      • Female
      • Goats
      • Horses
      • Kinetics
      • Macromolecular Substances
      • Milk / analysis
      • Peptide Fragments
      • Rabbits
      • Rats
      • Reindeer
      • Species Specificity

      Citations

      This article has been cited 1 times.
      1. Visser S, Jenness R, Mullin RJ. Isolation and characterization of beta- and gamma-caseins from horse milk. Biochem J 1982 Apr 1;203(1):131-9.
        doi: 10.1042/bj2030131pubmed: 6213224google scholar: lookup