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Enzymatic Activity in the M Band
Experiments which combined histochemistry and electron microscopy were performed in studying the sites of enzymatic hydrolysis of thiolacetic acid in the presence of lead ions in diaphragmatic and cardiac muscle. It was found that in these striated muscles the electron opaque, final product of the h...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1959
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229790/ https://www.ncbi.nlm.nih.gov/pubmed/13797093 |
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author | Barrnett, Russell J. Palade, George E. |
author_facet | Barrnett, Russell J. Palade, George E. |
author_sort | Barrnett, Russell J. |
collection | PubMed |
description | Experiments which combined histochemistry and electron microscopy were performed in studying the sites of enzymatic hydrolysis of thiolacetic acid in the presence of lead ions in diaphragmatic and cardiac muscle. It was found that in these striated muscles the electron opaque, final product of the histochemical reaction (PbS) was discretely deposited on the swelling of the thick elemental filaments that occurs at the M band. Additional sites of enzymatic activity occurred in mitrochondria and in round sarcoplasmic bodies. A reaction, probably non-enzymatic, also occurred in contraction bands in the area of the Z bands and in the sarcoplasmic reticulum. To ascertain the enzymatic nature of the reaction and to define the enzyme involved, control experiments were carried out and the effect of various esterase inhibitors was assayed. It is suggested that the M band enzyme is a cholinesterase, but the enzymes in the mitochondria and the sarcoplasmic bodies that hydrolyze the substrate appear to be different. A possible role of the M band enzyme is discussed. |
format | Text |
id | pubmed-2229790 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1959 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22297902008-05-01 Enzymatic Activity in the M Band Barrnett, Russell J. Palade, George E. J Biophys Biochem Cytol Article Experiments which combined histochemistry and electron microscopy were performed in studying the sites of enzymatic hydrolysis of thiolacetic acid in the presence of lead ions in diaphragmatic and cardiac muscle. It was found that in these striated muscles the electron opaque, final product of the histochemical reaction (PbS) was discretely deposited on the swelling of the thick elemental filaments that occurs at the M band. Additional sites of enzymatic activity occurred in mitrochondria and in round sarcoplasmic bodies. A reaction, probably non-enzymatic, also occurred in contraction bands in the area of the Z bands and in the sarcoplasmic reticulum. To ascertain the enzymatic nature of the reaction and to define the enzyme involved, control experiments were carried out and the effect of various esterase inhibitors was assayed. It is suggested that the M band enzyme is a cholinesterase, but the enzymes in the mitochondria and the sarcoplasmic bodies that hydrolyze the substrate appear to be different. A possible role of the M band enzyme is discussed. The Rockefeller University Press 1959-10-01 /pmc/articles/PMC2229790/ /pubmed/13797093 Text en Copyright © Copyright, 1959, by The Rockefeller Institute |
spellingShingle | Article Barrnett, Russell J. Palade, George E. Enzymatic Activity in the M Band |
title | Enzymatic Activity in the M Band |
title_full | Enzymatic Activity in the M Band |
title_fullStr | Enzymatic Activity in the M Band |
title_full_unstemmed | Enzymatic Activity in the M Band |
title_short | Enzymatic Activity in the M Band |
title_sort | enzymatic activity in the m band |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2229790/ https://www.ncbi.nlm.nih.gov/pubmed/13797093 |
work_keys_str_mv | AT barrnettrussellj enzymaticactivityinthemband AT paladegeorgee enzymaticactivityinthemband |