Interaction of aldolase with the troponin tropomyosin complex of bovine muscle

Clarke F.M., Masters C.J. and Winzor D.J. (1974) Interaction of aldolase with the troponin tropomyosin complex of bovine muscle. Biochemical Journal, 139 3: 785-788. doi:10.1042/bj1390785


Author Clarke F.M.
Masters C.J.
Winzor D.J.
Title Interaction of aldolase with the troponin tropomyosin complex of bovine muscle
Journal name Biochemical Journal   Check publisher's open access policy
ISSN 0264-6021
Publication date 1974-01-01
Sub-type Article (original research)
DOI 10.1042/bj1390785
Open Access Status Not yet assessed
Volume 139
Issue 3
Start page 785
End page 788
Total pages 4
Language eng
Subject 1303 Specialist Studies in Education
Abstract Ultracentrifugal studies of mixtures of aldolase and the troponin/tropomyosin complex from bovine muscle showed the existence of a labile interaction between these 2 myofibrillar constituents in amidazole buffers, pH6.8, I 0.02 to 0.10 (mol/l), and the suppression of the reaction by fructose 1,6 diphosphate. Analysis of the sedimentation velocity patterns suggests the binding of more than 2 molecules of troponin / tropomyosin / molecule of aldolase. The results illustrate the necessity of considering additional or alternative sites to F actin to account for the observed binding of aldolase to the thin filaments of skeletal muscle.
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
 
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Created: Tue, 30 Aug 2016, 13:10:56 EST by System User