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Molecular and cellular biochemistry1980; 29(1); 3-9; doi: 10.1007/BF00230951

Comparative studies of alpha-lactalbumin and lysozyme: the proteins of kangaroo (Megaleia rufa and Macropus giganteus) and horse (Equus caballus).

Abstract: As part of a study of the 'whey' proteins of various mammals, a comparison is made of the alpha-lactalbumins and lysozymes of the kangaroo and horse. In the milk of the red kangaroo (Megaleia rufa) there is only one alpha-lactalbumin and it occurs throughout lactation, but no lysozyme has been detected. There are two alpha-lactalbumins in the milk of the grey kangaroo (Macropus giganteus), one, designated alpha-lactalbumin Zone B, is present throughout lactation; the second, designated alpha-lactalbumin Zone A, is present only in late lactation. One lysozyme is also present. The milk of the horse (Equus caballus) contains one alpha-lactalbumin and at least one lysozyme. Partial amino acid sequences are proposed from sequence determination and from analyses of tryptic peptides compared with the known sequences of other alpha-lactalbumins and lysozymes.
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Publication Date: 1980-01-16 PubMed ID: 7366582DOI: 10.1007/BF00230951Google Scholar: Lookup
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  • Comparative Study
  • Journal Article

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article presents a comparative analysis of alpha-lactalbumins and lysozymes in the milk of kangaroos and horses, aiming to understand the variations in ‘whey’ proteins across different mammal species.

Objective of the Study

  • The main objective of the paper is to study and compare the alpha-lactalbumins and lysozymes present in the milk of large marsupials (kangaroos – Megaleia rufa and Macropus giganteus) and a large domestic mammal (horse – Equus caballus).

Study Findings and Observations

  • The researchers found that the milk of the red kangaroo contains only one type of alpha-lactalbumin present throughout the lactation period, but no lysozyme was detected.
  • Grey kangaroo milk contains two types of alpha-lactalbumins; alpha-lactalbumin Zone B is found throughout lactation, while alpha-lactalbumin Zone A is only present in the late stages of lactation. They also detected a type of lysozyme in grey kangaroo milk.
  • Horse milk, in comparison, is found to contain one alpha-lactalbumin and at least one type of lysozyme, displaying similarity with grey kangaroo in terms of lysozyme presence.

Methods Employed in the Research

  • To identify the specific types of these proteins and their presence at different stages of lactation in each animal, the researchers carried out partial sequence determination and tryptic peptide analysis.
  • The structural changes in the alpha-lactalbumins and lysozymes throughout the stages of lactation were studied by comparing the determined amino acid sequences with known sequences of these proteins from other existing species’ milk.

Significance of the Study

  • These findings can be useful to understand the unique biological and chemical characteristics of marsupial milk in comparison to large mammals—a valuable knowledge contribution to the field of biomolecular and comparative evolutionary research.

Cite This Article

APA
Bell K, McKenzie HA, Muller V, Shaw DC. (1980). Comparative studies of alpha-lactalbumin and lysozyme: the proteins of kangaroo (Megaleia rufa and Macropus giganteus) and horse (Equus caballus). Mol Cell Biochem, 29(1), 3-9. https://doi.org/10.1007/BF00230951

Publication

Molecular and cellular biochemistry
ISSN: 0300-8177
NlmUniqueID: 0364456
Country: Netherlands
Language: English
Volume: 29
Issue: 1
Pages: 3-9

Researcher Affiliations

Bell, K
    McKenzie, H A
      Muller, V
        Shaw, D C

          MeSH Terms

          • Amino Acid Sequence
          • Animals
          • Cattle
          • Electrophoresis, Starch Gel
          • Female
          • Guinea Pigs
          • Horses / physiology
          • Humans
          • Lactalbumin / analysis
          • Lactation
          • Macropodidae / physiology
          • Marsupialia / physiology
          • Milk / analysis
          • Molecular Weight
          • Muramidase / analysis
          • Pregnancy

          References

          This article includes 17 references
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          Citations

          This article has been cited 3 times.
          1. Herrouin M, Mollé D, Fauquant J, Ballestra F, Maubois JL, Léonil J. New genetic variants identified in donkey's milk whey proteins. J Protein Chem 2000 Feb;19(2):105-15.
            doi: 10.1023/a:1007078415595pubmed: 10945434google scholar: lookup
          2. Bell K, McKenzie HA, Shaw DC. Porcine alpha-lactalbumin A and B. Mol Cell Biochem 1981 Mar 13;35(2):113-9.
            doi: 10.1007/BF02354825pubmed: 7231400google scholar: lookup
          3. Nicholas KR, Messer M, Elliott C, Maher F, Shaw DC. A novel whey protein synthesized only in late lactation by the mammary gland from the tammar (Macropus eugenii). Biochem J 1987 Feb 1;241(3):899-904.
            doi: 10.1042/bj2410899pubmed: 3109381google scholar: lookup
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