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PMID: 127617 Published · ppublish English Journal Article

The immunological specificity of myosins from cross-striated muscles as revealed by quantitative microcomplement fixation and enzyme inhibition by antisera.

Biochimica et biophysica acta ·Vol. 412 ·No. 1 ·1975-11-18 ·Pages 39-50

Bruggmann S, Jenny E

Abstract

The immunological properties of myosins, especially their muscle-type, class and species specificity, are still controversial. It is the opinion of the authors that the lack of agreement might at least in part be due to the use of contaminated myosins as immunogens and inappropriate methods. We, therefore, purified myosins to a very high degree (approximately 99%) and induced antisera in guinea-pigs. Studies of quantitative microcomplement fixation and enzyme-inhibition by antisera yielded the following results: myosins of cross-striated muscle have an absolute class, a very pronounced muscle-type and a low species specificity. It can be shown that even a very small contamination of myosins with other proteins could seriously hamper the experiments and that the results obtained depend significantly on the immunological methods employed.

MeSH Terms
Adenosine Triphosphatases/metabolism Animals Chickens Complement Fixation Tests Dogs Ethylmaleimide Immune Sera Molecular Weight Muscles/analysis Myocardium/analysis Myofibrils/analysis Myosins/analysis,immunology Organ Specificity Precipitin Tests Protein Binding Rabbits Species Specificity Swine
Chemicals
Immune Sera Adenosine Triphosphatases Myosins Ethylmaleimide
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Bruggmann S
Jenny E
Article Info
Journal
Biochimica et biophysica acta
Abbr.
Biochim Biophys Acta
ISSN
0006-3002
Published
1975-11-18
Pages
39-50
Language
English
Region
Netherlands
NLM ID
0217513
Subset
IM
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