FREE SHIPPING over $40
OVER 9000 FIVE-STAR REVIEWS
5% OFF ALL SUBSCRIPTIONS
100% HAPPINESS GUARANTEE
Analyze Diet
0
Home / Equine Research Bank / Histochemistry / Structural, histochemical and biochemical observations on ho...
Histochemistry1988; 88(3-6); 357-365; doi: 10.1007/BF00570295

Structural, histochemical and biochemical observations on horse milk-fat-globule membranes and casein micelles.

Abstract: Horse milk fat globules (MFGs) and casein micelles were studied using freeze fracturing, freeze etching and thin-section electron microscopy, as well as lectin histochemistry, gel electrophoresis, and Western blotting. Horse MFGs were found to be relatively small, their average volume-surface diameter being about 2.75 microns. The MFG membrane is composed of three layers: an inner proteinaceous coat occasionally having a paracrystalline substructure, a unit membrane, and a prominent filamentous glycocalyx. The last is rich in glycoconjugates, as revealed by its binding of various lectins. In addition, the glycocalyx binds cationized ferritin, which indicates the presence of negative electric charges. Gel electrophoresis revealed the presence of high-molecular-weight glycoproteins in the MFG membrane of horse milk. Such glycoproteins are also present in human MFG membranes but are absent in the bovine MFGs. The casein micelles in horse milk are relatively large, their average volume-surface diameter being about 200 nm.
Get Full Text
Publication Date: 1988-01-01 PubMed ID: 3366639DOI: 10.1007/BF00570295Google 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
  • Research Support
  • Non-U.S. Gov't

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.

This research article examines the structural, histochemical and biochemical properties of fat globules and casein micelles in horse milk using state of the art microscopy techniques and biochemical tests. Findings revealed that horse milk fat globules are smaller than others, they have a distinct three-layered membrane structure, with presence of high molecular weight glycoproteins. This structure differs from those in human or bovine milk.

Explanation of Research

The authors set out to study the microscopic and biochemical properties of horse milk, with a particular focus on milk fat globules (MFGs) and casein micelles. These particles give milk its creaminess and also carry important nutrients. Researchers used a variety of advanced analytical techniques to carry out this task.

  • Freeze fracturing, freeze etching and thin-section electron microscopy: These techniques helped provide a detailed look at the structure of horse milk’s MFGs and casein micelles. Initial result showed that MFGs were relatively small in size.
  • Lectin histochemistry: This is a technique used to detect glycoconjugates, complex molecules present in the MFG. The test revealed the presence of these molecules, indicating that the MFG membrane is rich in glycoconjugates.
  • Gel electrophoresis and Western blotting: These techniques were used to profile the different protein types present in the MFGs. They showed high-molecular-weight glycoproteins in the MFG membrane.

Findings from the Research

  • The MFGs in horse milk were found to have a distinct three-layered structure. The outer layer or glycocalyx was found to be rich in glycoconjugates. It also binds cationized ferritin, indicating the influence of negative electric charges.
  • Apart from glycoconjugates, the MFG membrane also demonstrated the presence of high-molecular-weight glycoproteins. These were detected through the use of gel electrophoresis. In comparison, these glycoproteins were also found in human milk, but absent in bovine milk.
  • Another significant finding was the size of casein micelles, which were relatively large compared to other species. The exact significance of this difference is not elaborated in the abstract.

Overall, the study provides a detailed picture of the structure and makeup of MFGs and casein micelles in horse milk thereby extending our understanding of the uniqueness and potential nutritional benefits of this milk type.

Cite This Article

APA
Welsch U, Buchheim W, Schumacher U, Schinko I, Patton S. (1988). Structural, histochemical and biochemical observations on horse milk-fat-globule membranes and casein micelles. Histochemistry, 88(3-6), 357-365. https://doi.org/10.1007/BF00570295

Publication

Histochemistry
ISSN: 0301-5564
NlmUniqueID: 0411300
Country: Germany
Language: English
Volume: 88
Issue: 3-6
Pages: 357-365

Researcher Affiliations

Welsch, U
  • Anatomische Anstalt, Lehrstuhl II, Ludwig-Maximilians-Universität, München, Federal Republic of Germany.
Buchheim, W
    Schumacher, U
      Schinko, I
        Patton, S

          MeSH Terms

          • Animals
          • Caseins / metabolism
          • Cattle
          • Female
          • Histocytochemistry
          • Horses / metabolism
          • Humans
          • Lectins
          • Membrane Glycoproteins / metabolism
          • Micelles
          • Microscopy, Electron
          • Milk / metabolism
          • Mucin-1
          • Pregnancy
          • Species Specificity

          References

          This article includes 16 references
          1. Shimizu M, Yamauchi K, Miyauchi Y, Sakurai T, Tokugawa K, McIlhinney RA. High-Mr glycoprotein profiles in human milk serum and fat-globule membrane.. Biochem J 1986 Feb 1;233(3):725-30.
            pubmed: 3707520doi: 10.1042/bj2330725google scholar: lookup
          2. 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.
            pubmed: 6213224doi: 10.1042/bj2030131google scholar: lookup
          3. KALLIALA H, SELESTE E, HALLMAN N. On the use of mare's milk in infant feeding.. Acta Paediatr (Stockh) 1951 Mar;40(2):94-117.
            pubmed: 14829256doi: 10.1111/j.1651-2227.1951.tb15789.xgoogle scholar: lookup
          4. Ullrey DE, Struthers RD, Hendricks DG, Brent BE. Composition of mare's milk.. J Anim Sci 1966 Feb;25(1):217-22.
            pubmed: 5910963doi: 10.2527/jas1966.251217xgoogle scholar: lookup
          5. Goldstein IJ, Hayes CE. The lectins: carbohydrate-binding proteins of plants and animals.. Adv Carbohydr Chem Biochem 1978;35:127-340.
            pubmed: 356549doi: 10.1016/s0065-2318(08)60220-6google scholar: lookup
          6. Patton S, Huston GE. Differences between individuals in high-Mr glycoproteins from human mammary epithelia.. FEBS Lett 1987 May 25;216(1):151-4.
            pubmed: 3582663doi: 10.1016/0014-5793(87)80774-3google scholar: lookup
          7. Shimizu M, Yamauchi K. Isolation and characterization of mucin-like glycoprotein in human milk fat globule membrane.. J Biochem 1982 Feb;91(2):515-24.
            pubmed: 7068573doi: 10.1093/oxfordjournals.jbchem.a133724google scholar: lookup
          8. Horisberger M, Rosset J, Vonlanthen M. Location of glycoproteins on milk fat globule membrane by scanning and transmission electron microscopy, using lectin-labelled gold granules.. Exp Cell Res 1977 Oct 15;109(2):361-9.
            pubmed: 562271doi: 10.1016/0014-4827(77)90015-5google scholar: lookup
          9. Moroi M, Jung SM. Selective staining of human platelet glycoproteins using nitrocellulose transfer of electrophoresed proteins and peroxidase-conjugated lectins.. Biochim Biophys Acta 1984 Apr 24;798(3):295-301.
            pubmed: 6201194doi: 10.1016/0304-4165(84)90101-6google scholar: lookup
          10. Buchheim W. Paracrystalline arrays of milk fat globule membrane-associated proteins as revealed by freeze-fracture.. Naturwissenschaften 1982 Oct;69(10):505-7.
            pubmed: 7144921doi: 10.1007/BF00365826google scholar: lookup
          11. BARGMANN W, KNOOP A. [Morphology of lactation; light & electro-microscopic studies on the mammary glands of rats].. Z Zellforsch Mikrosk Anat 1959;49(3):344-88.
            pubmed: 13648715
          12. Donnelly WJ, McNeill GP, Buchheim W, McGann TC. A comprehensive study of the relationship between size and protein composition in natural bovine casein micelles.. Biochim Biophys Acta 1984 Sep 11;789(2):136-43.
            pubmed: 6477926doi: 10.1016/0167-4838(84)90197-3google scholar: lookup
          13. Oftedal OT, Hintz HF, Schryver HF. Lactation in the horse: milk composition and intake by foals.. J Nutr 1983 Oct;113(10):2096-106.
            pubmed: 6619986doi: 10.1093/jn/113.10.2096google scholar: lookup
          14. Jenness R. The composition of human milk.. Semin Perinatol 1979 Jul;3(3):225-39.
            pubmed: 392766
          15. Patton S, Huston GE. A method for isolation of milk fat globules.. Lipids 1986 Feb;21(2):170-4.
            pubmed: 3959776doi: 10.1007/BF02534441google scholar: lookup
          16. Buchheim W, Welsch U, Huston GE, Patton S. Glycoprotein filament removal from human milk fat globules by heat treatment.. Pediatrics 1988 Jan;81(1):141-6.
            pubmed: 3336582

          Citations

          This article has been cited 4 times.
          1. Penhaligan J, Poppitt SD, Miles-Chan JL. The Role of Bovine and Non-Bovine Milk in Cardiometabolic Health: Should We Raise the "Baa"?. Nutrients 2022 Jan 11;14(2).
            doi: 10.3390/nᐂ0290pubmed: 35057470google scholar: lookup
          2. Notarianni LJ, Belk D, Aird SA, Bennett PN. An in vitro technique for the rapid determination of drug entry into breast milk.. Br J Clin Pharmacol 1995 Oct;40(4):333-7.
            doi: 10.1111/j.1365-2125.1995.tb04555.xpubmed: 8554935google scholar: lookup
          3. Zeller U, Richter J. The monoptychic glands of the jugulo-sternal scent gland field of Tupaia: a TEM and SEM study.. J Anat 1990 Oct;172:25-38.
            pubmed: 2272906
          4. Schumacher U, Trudrung P, Ruhnke M, Gossrau R. Direct tissue isoelectric focusing on ultrathin polyacrylamide gels. Applications in enzyme, lectin and immunohistochemistry.. Histochem J 1990 Aug;22(8):433-8.
            doi: 10.1007/BF01003463pubmed: 1699914google scholar: lookup
          Subscribe to our newsletter
          Join 99,383 horse owners like you who receive our email updates on horse health and nutrition.