|Author||Appukuttan, P. S. ♦ Basu, D.|
|Source||Sree Chitra Tirunal Institute for Medical Sciences & Technology|
|Publisher||Indian Journal of Biochemistry & Biophysics|
|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|
|Abstract||Creatine kinase (ATP: creatine N-phosphotransferase, EC 188.8.131.52) 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)|
|Journal||INDIAN JOURNAL OF BIOCHEMISTRY & BIOPHYSICS|
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