Functional non-identity of creatine kinase subunits of rabbit skeletal muscle

The authors have separated the different subunits of creatine kinase (CK) by affinity chromatography on Sepharose containing an immobilized analog of ATP, after dissociation of CK into subunits by 5 M urea, and have shown their functional non-identity.

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Bibliographic Details
Published inFEBS letters Vol. 149; no. 1; pp. 36 - 40
Main Authors Nevinsky, G.A., Ankilova, V.N., Lavrik, O.I., Mkrtchyan, Z.S., Nersesova, L.S., Akopyan, J.I.
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 22.11.1982
Subjects
6-(4-toluidino)-2-naphthalenesulfonic acid
Active centre identity
Animals
azido-ATP
creatine kinase
creatine kinase (EC 2.7.3.2)
Creatine Kinase - isolation & purification
Creatine kinase subunit
fractionation
Functional non-identity
Hepes
Hydrogen-Ion Concentration
Kinetics
Macromolecular Substances
Muscles - enzymology
N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid
Phosphorylation
Rabbit skeletal muscle
Rabbits
skeletal muscle
Subunit function
TNS
Transphosphorylation
γ-(p-azidoanilide)-ATP
Rabbit skeletal muscle
Creatine kinase subunit
Functional non-identity
Subunit function
Active centre identity
Hepes
Transphosphorylation
CK
TNS
azido-ATP
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Summary:The authors have separated the different subunits of creatine kinase (CK) by affinity chromatography on Sepharose containing an immobilized analog of ATP, after dissociation of CK into subunits by 5 M urea, and have shown their functional non-identity.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(82)81065-X