Enzyme kinetic evidence of active-site involvement in the interaction between aldolase and muscle myofibrils

Harris S.J. and Winzor D.J. (1987) Enzyme kinetic evidence of active-site involvement in the interaction between aldolase and muscle myofibrils. Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 911 1: 121-126. doi:10.1016/0167-4838(87)90279-2


Author Harris S.J.
Winzor D.J.
Title Enzyme kinetic evidence of active-site involvement in the interaction between aldolase and muscle myofibrils
Journal name Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
ISSN 0167-4838
Publication date 1987-01-05
Sub-type Article (original research)
DOI 10.1016/0167-4838(87)90279-2
Volume 911
Issue 1
Start page 121
End page 126
Total pages 6
Subject 1303 Specialist Studies in Education
1304 Biophysics
1312 Molecular Biology
1315 Structural Biology
Abstract The interaction of aldolase with the myofibrillar matrix of rabbit skeletal muscle has been investigated by means of its effect on kinetic parameters for the enzyme-catalyzed cleavage of fructose 1,6-bisphosphate. Involvement of the active site in the enzymic interaction with the thin filament of muscle is indicated, the association constant for competitive inhibition of catalysis (420 000 M-1) being in excellent agreement with the value of 410 000 M-1 obtained under the same conditions (pH 6.8, I 0.16) from partition equilibrium studies of the aldolase-myofibril interaction (Kuter, M.R., Masters, C.J. and Winzor, D.J. (1983) Arch. Biochem. Biophys. 225, 384-389). A second kinetic study, designed to take into greater account the inhibitory effects of substrate and other phosphate-containing metabolites on the interaction of enzyme with myofibrils, has substantiated further the concept of aldolase existing as an equilibrium mixture of cytoplasmic and filament-bound forms in muscle tissue.
Keyword Aldolase-myofibril interaction
Enzyme kinetics
Fructose 1,6-bisphosphate
Q-Index Code C1
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Scopus Import - Archived
 
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