On the association of glycolytic enzymes with structural proteins of skeletal muscle

Clarke F.M. and Masters C.J. (1975) On the association of glycolytic enzymes with structural proteins of skeletal muscle. BBA - General Subjects, 381 1: 37-46. doi:10.1016/0304-4165(75)90187-7

Author Clarke F.M.
Masters C.J.
Title On the association of glycolytic enzymes with structural proteins of skeletal muscle
Journal name BBA - General Subjects   Check publisher's open access policy
ISSN 0304-4165
Publication date 1975-01-13
Sub-type Article (original research)
DOI 10.1016/0304-4165(75)90187-7
Open Access Status Not yet assessed
Volume 381
Issue 1
Start page 37
End page 46
Total pages 10
Language eng
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
2700 Medicine
Abstract 1. 1. The effects of protein concentration and ionic strength on the adsorption of the individual glycolytic enzymes to F-actin and F-actin-trypomyosin-troponin have been studied. 2. 2. Appreciable association was demonstrated under conditions of physiological ionic strength and high protein concentration, and tropomyosin-troponin established as an important and generalized component of these interactions. 3. 3. Phosphofructokinase, aldolase, pyruvate kinase, lactate dehydrogenase, glyceraldehyde-3-phosphate dehydrogenase and glucose-6-phosphate isomerase were strongly bound under these conditions, while triosephosphate isomerase, phosphoglycerate kinase, phosphoglycerate mutase, enolase and hexokinase displayed less adsorption to the structural proteins. 4. 4. The influence of a number of parameters on the adsorption phenomena was examined. Ca2+ and fructose 1,6-diphosphate increased the adsorption of aldolase, lactate dehydrogenase and pyruvate kinase, while decreasing the adsorption of the enzymes of the constant-proportion group. 5. 5. Of the other major enzymic components of skeletal muscle, creatine kinase, adenylate kinase and malate dehydrogenase showed no adsorption to F-actin-tropomyosin-troponin under the experimental conditions. Some adsorption was evident, however, in the case of aspartate aminotransferase, (NADP) isocitrate dehydrogenase and α-glycerolphosphate dehydrogenase. 6. 6. These results have been discussed in relation to their functional significance and the roles of enzyme compartmentation in the cell.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
Version Filter Type
Citation counts: Scopus Citation Count Cited 171 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 28 Jun 2016, 15:47:06 EST by System User