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The Biochemical journal1966; 100(1); 6C-7C; doi: 10.1042/bj1000006c

Comparative studies on the soluble protein fractions of bovine, equine, porcine and ovine adrenal chromaffin granules.

Abstract: No abstract available.
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Publication Date: 1966-07-01 PubMed ID: 4960872PubMed Central: PMC1265126DOI: 10.1042/bj1000006cGoogle Scholar: Lookup
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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.

Objective Overview

Comparative studies were conducted on the soluble protein fractions of adrenal chromaffin granules in bovine, equine, porcine, and ovine species. The research explores the release mechanism of catecholamines and the structural relationships between granular soluble proteins in these animal species.

Isolation and Extraction

  • Chromaffin granules were isolated from the adrenal medulla of ox, horse, pig, and sheep, with modifications to the method described by Blaschko, Hagen & Hagen (1957).
  • The `large-granule’ fraction obtained by differential centrifugation was further resolved by layering samples on sucrose, followed by ultracentrifugation.
  • Granular soluble protein fractions were extracted by resuspending granular pellets in water and then centrifuging the suspensions.
  • Protein recoveries as granular soluble protein were determined for each species.

Antigenic Activities and Concentration

  • Protein preparations from ovine and porcine origins were concentrated using Sephadex G-25 to achieve protein concentrations of 0.2-1.0%.
  • Antigenic activities of soluble protein preparations were tested using rabbit antiserum against bovine soluble protein on Ouchterlony plates.
  • Precipitation lines were observed for all four species, indicating antigen-antibody reactions.

Immunological Analysis and Precipitation Patterns

  • Immunological analysis revealed that bovine soluble protein appeared identical to ovine origin but exhibited inhibition patterns with equine and porcine soluble protein fractions.
  • Antigen-antibody precipitation patterns indicated a multicomponent system in bovine soluble protein, with shared determinants between bovine and ovine preparations.
  • Electrophoresis of soluble protein fractions showed distinct mobility patterns, with two hypersharp lines for bovine origin and two to three fine lines for the other species.

Identification of Immunologically Active Components

  • The immunological analysis, combined with electrophoresis results, confirmed the existence of two immunologically active components, a and b, in bovine soluble protein.
  • Components a and b were found to be immunologically indistinguishable from those of ovine origin.
  • Component b appeared immunologically unrelated to components present in equine and porcine soluble protein.

Confirmation by Starch-Gel Electrophoresis

  • Recent observations on starch-gel electrophoresis supported the finding of one main component shared by the investigated species and other distinct components in ox, horse, and pig.

The research provides detailed insights into the structural relationships and immunological characteristics of soluble protein fractions in adrenal chromaffin granules across different mammalian species.

Cite This Article

APA
Helle KB. (1966). Comparative studies on the soluble protein fractions of bovine, equine, porcine and ovine adrenal chromaffin granules. Biochem J, 100(1), 6C-7C. https://doi.org/10.1042/bj1000006c

Publication

The Biochemical journal
ISSN: 0264-6021
NlmUniqueID: 2984726R
Country: England
Language: English
Volume: 100
Issue: 1
Pages: 6C-7C

Researcher Affiliations

Helle, K B

    MeSH Terms

    • Adrenal Glands / analysis
    • Animals
    • Cattle
    • Chromaffin System / analysis
    • Horses
    • Immune Sera
    • Immunodiffusion
    • Precipitin Tests
    • Proteins / analysis
    • Rabbits
    • Sheep
    • Swine

    References

    This article includes 6 references
    1. Douglas WW, Poisner AM. Evidence that the secreting adrenal chromaffin cell releases catecholamines directly from ATP-rich granules.. J Physiol 1966 Mar;183(1):236-48.
      pubmed: 5945251doi: 10.1113/jphysiol.1966.sp007863google scholar: lookup
    2. Helle K. Antibody formation against soluble protein from bovine adrenal chromaffin granules.. Biochim Biophys Acta 1966 Mar 28;117(1):107-10.
      pubmed: 4958302doi: 10.1016/0304-4165(66)90157-7google scholar: lookup
    3. COUPLAND RE. (ELECTRON MICROSCOPIC OBSERVATIONS ON THE STRUCTURE OF THE RAT ADRENAL MEDULLA. I. THE ULTRASTRUCTURE AND ORGANIZATION OF CHROMAFFIN CELLS IN THE NORMAL ADRENAL MEDULLA.).. J Anat 1965 Apr;99(Pt 2):231-54.
      pubmed: 14330730
    4. BLASCHKO H, HAGEN JM, HAGEN P. Mitochondrial enzymes and chromaffin granules.. J Physiol 1957 Dec 3;139(2):316-22.
      pubmed: 13492215doi: 10.1113/jphysiol.1957.sp005893google scholar: lookup
    5. POULIK MD. Starch gel electrophoresis in a discontinous system of buffers.. Nature 1957 Dec 28;180(4600):1477-9.
      pubmed: 13493570doi: 10.1038/1801477a0google scholar: lookup
    6. BLASCHKO H, BORN GV, D'IORIO A, EADE NR. Observations on the distribution of catechol amines and adenosinetriphosphate in the bovine adrenal medulla.. J Physiol 1956 Sep 27;133(3):548-57.
      pubmed: 13368103doi: 10.1113/jphysiol.1956.sp005607google scholar: lookup

    Citations

    This article has been cited 4 times.
    1. Baird PN, Saw SM, Lanca C, Guggenheim JA, Smith Iii EL, Zhou X, Matsui KO, Wu PC, Sankaridurg P, Chia A, Rosman M, Lamoureux EL, Man R, He M. Myopia. Nat Rev Dis Primers 2020 Dec 17;6(1):99.
      doi: 10.1038/s41572-020-00231-4pubmed: 33328468google scholar: lookup
    2. Ottesen AH, Christensen G, Omland T, Røsjø H. Glycosylated Chromogranin A: Potential Role in the Pathogenesis of Heart Failure. Curr Heart Fail Rep 2017 Dec;14(6):478-488.
      doi: 10.1007/s11897-017-0360-xpubmed: 28975588google scholar: lookup
    3. Hopwood D. An immunohistochemical study of the adrenal medulla of the ox. A comparison of antibodies against whole ox chromaffin granules and ox chromogranin A. Histochemie 1968;13(4):323-30.
      pubmed: 4972178
    4. Winkler H, Fischer-Colbrie R. The chromogranins A and B: the first 25 years and future perspectives. Neuroscience 1992 Aug;49(3):497-528.
      doi: 10.1016/0306-4522(92)90222-npubmed: 1501763google scholar: lookup
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