FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / Mol Cell Biochem / Comparative studies of alpha-lactalbumin and lysozyme: the p...
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.
Get Full Text
Publication Date: 1980-01-16 PubMed ID: 7366582DOI: 10.1007/BF00230951Google Scholar: Lookup
The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
LinkedInCopy
  • 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
          1. Stephens T, Irvine S, Mutton P, Gupta JD, Marley JD. Deficiency of two enzymes of galactose metabolism in kangaroos.. Nature 1974 Apr 5;248(448):524-5.
            pubmed: 4824350doi: 10.1038/248524a0google scholar: lookup
          2. Hopper KE, McKenzie HA. Comparative studies of alpha-lactalbumin and lysozyme: Echidna lysozyme.. Mol Cell Biochem 1974 Apr 15;3(2):93-108.
            pubmed: 4208938doi: 10.1007/BF01659181google scholar: lookup
          3. Jollès J, Jollès P. Comparison between human and bird lysozymes: Note concerning the previously observed deletion.. FEBS Lett 1972 Apr 15;22(1):31-33.
            pubmed: 11946553doi: 10.1016/0014-5793(72)80211-4google scholar: lookup
          4. Brodbeck U, Denton WL, Tanahashi N, Ebner KE. The isolation and identification of the B protein of lactose synthetase as alpha-lactalbumin.. J Biol Chem 1967 Apr 10;242(7):1391-7.
            pubmed: 6023212
          5. Bell K, Hopper KE, McKenzie HA, Murphy WH, Shaw DC. A comparison of bovine alpha-lactalbumin A and B of Droughtmaster.. Biochim Biophys Acta 1970 Sep 29;214(3):437-44.
            pubmed: 5534301doi: 10.1016/0005-2795(70)90302-8google scholar: lookup
          6. Brew K, Castellino FJ, Vanaman TC, Hill RL. The complete amino acid sequence of bovine alpha-lactalbumin.. J Biol Chem 1970 Sep 10;245(17):4570-82.
            pubmed: 5532231
          7. Mendez E, Lai CY. Regeneration of amino acids from thiazolinones formed in the Edman degradation.. Anal Biochem 1975 Sep;68(1):47-53.
            pubmed: 242232doi: 10.1016/0003-2697(75)90677-6google scholar: lookup
          8. Brew K, Campbell PN. The characterization of the whey proteins of guinea-pig milk. The isolation and properties of alpha-lactalbumin.. Biochem J 1967 Jan;102(1):258-64.
            pubmed: 6030288doi: 10.1042/bj1020258google scholar: lookup
          9. Brodbeck U, Ebner KE. Resolution of a soluble lactose synthetase into two protein components and solubilization of microsomal lactose synthetase.. J Biol Chem 1966 Feb 10;241(3):762-4.
            pubmed: 5908140
          10. PARRY RM Jr, CHANDAN RC, SHAHANI KM. A RAPID AND SENSITIVE ASSAY OF MURAMIDASE.. Proc Soc Exp Biol Med 1965 Jun;119:384-6.
            pubmed: 14328897doi: 10.3181/00379727-119-30188google scholar: lookup
          11. Brew K, Steinman HM, Hill RL. A partial amino acid sequence of -lactalbumin-I of the grey kangaroo (Macropus giganteus).. J Biol Chem 1973 Jul 10;248(13):4739-42.
            pubmed: 4718741
          12. Jauregui-Adell J, Cladel G, Ferraz-Pina C, Rech J. Isolation and partial characterization of mare milk lysozyme.. Arch Biochem Biophys 1972 Jul;151(1):353-5.
            pubmed: 5044524doi: 10.1016/0003-9861(72)90507-3google scholar: lookup
          13. Brew K. The complete amino-acid sequence of guinea-pig -lactalbumin.. Eur J Biochem 1972 May 23;27(2):341-53.
            pubmed: 5065784doi: 10.1111/j.1432-1033.1972.tb01844.xgoogle scholar: lookup
          14. Bailey LF, Lemon M. Specific milk proteins associated with resumption of development by the quiescent blastocyst of the lactating red kangaroo.. J Reprod Fertil 1966 Jun;11(3):473-5.
            pubmed: 5949521doi: 10.1530/jrf.0.0110473google scholar: lookup
          15. Hill RL, Brew K. Lactose synthetase.. Adv Enzymol Relat Areas Mol Biol 1975;43:411-90.
            pubmed: 812340doi: 10.1002/9780470122884.ch5google scholar: lookup
          16. Fitzgerald DK, Colvin B, Mawal R, Ebner KE. Enzymic assay for galactosyl transferase activity of lactose synthetase and alpha-lactalbumin in purified and crude systems.. Anal Biochem 1970 Jul;36(1):43-61.
            pubmed: 5482638doi: 10.1016/0003-2697(70)90330-1google scholar: lookup
          17. Findlay JB, Brew K. The complete amino-acid sequence of human -lactalbumin.. Eur J Biochem 1972 May;27(1):65-86.
            pubmed: 5049057doi: 10.1111/j.1432-1033.1972.tb01812.xgoogle scholar: lookup

          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
          Subscribe to our newsletter
          Join 99,357 horse owners like you who receive our email updates on horse health and nutrition.