Isolation and some properties of troponin T kinase from rabbit skeletal muscle

A method for isolation of troponin T kinase (ATP-protein phosphotransferase, EC 2.7.1.37) from rabbit skeletal muscles in proposed. The method gives a 7000-10 000-fold purification and results in an enzyme with specific activity of 400-800-nmol x min-1 x mg-1 of protein. The molecular weight of trop...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical journal 1980-08, Vol.189 (2), p.219-226
Main Authors: Gusev, N B, Dobrovolskii, A B, Severin, S E
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Chromatography, Gel
Chromatography, Ion Exchange
Molecular Weight
Muscle Proteins - analysis
Muscles - enzymology
Phosphorylation
Protein Kinases - isolation & purification
Rabbits
Substrate Specificity
Troponin - isolation & purification
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A method for isolation of troponin T kinase (ATP-protein phosphotransferase, EC 2.7.1.37) from rabbit skeletal muscles in proposed. The method gives a 7000-10 000-fold purification and results in an enzyme with specific activity of 400-800-nmol x min-1 x mg-1 of protein. The molecular weight of tropin T kinase as determined by gel filtration exceeds 500 000. Electrophoresis in polyacrylamide gel in the presence of sodium dodecyl sulphate revealed that isolated preparations of the enzyme consisted of at least three distinct proteins with apparent mol.wt. of 50 000, 46 000 and 31 000. The enzyme phosphorylates isolated troponin T at a rate which exceeds the phosphorylation rates of casein, phosvitin, histones, phosphorylase b and protamine 5-30-fold. Within the whole troponin complex, only troponin T is phosphorylated by the enzyme. The enzyme phosphorylates only the N-terminal serine residue of troponin T, i.e. the site that is normally phosphorylated in the whole troponin complex isolated from rabbit skeletal muscles.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj1890219