Access Restriction

Author Appukuttan, P. S. ♦ Basu, D.
Source Sree Chitra Tirunal Institute for Medical Sciences & Technology
Content type Text
Publisher Indian Journal of Biochemistry & Biophysics
File Format PDF
Language English
Subject Domain (in DDC) Natural sciences & mathematics ♦ Life sciences; biology ♦ Physiology & related subjects ♦ Biochemistry ♦ Technology ♦ Medicine & health
Subject Domain (in MeSH) Enzymes and Coenzymes ♦ Chemicals and Drugs ♦ Physical Phenomena ♦ Chemical Phenomena ♦ Biological Sciences
Subject Keyword Biochemistry
Abstract Creatine kinase (ATP: creatine N-phosphotransferase, EC from adult human brain grey matter was purified by cibacron blue F3GA-Sepharose affinity chromatography. By gel electrophoresis of the purified enzyme under non-denaturing conditions a single protein band was observed. The dye-bound enzyme was eluted using its substrate, ATP. Reversibility of the binding of purified creatine kinase to blue Sepharose by ATP in a concentration-dependent manner indicated that the cibacron blue molecule which structurally mimics nucleotides occupied the substrate binding site of the enzyme. Also the marked dependence of enzyme binding to blue Sepharose on Mg2+ concentration suggested that Mg2+ ion is capable of combining with the dye moiety to form a site-specific binding complex that is similar to the physiological substrate of creatine kinase, namely Mg2+-ATP or Mg2+-ADP.
Education Level UG and PG
Learning Resource Type Article
Educational Framework Medical Council of India (MCI)
Volume Number 29
Issue Number 4
Page Count 4
Starting Page 346
Ending Page 349