Comparison of enzymatic characteristics of creatine kinase BB from human healthy and tumor stomach tissues.

Abstract

Creatine kinase (ATP: creatine N-phosphotransferase, EC 2.7.3.2, CK) BB isoenzyme from stomach tumor tissue was partially purified and its characteristics were compared with those from healthy tissue. Molecular mass of tumor CK-BB was estimated to be 82 000 by polyacrylamide gel electrophoresis. Tumor CK-BB was separated into 2 main subbands around pH 4.5 and 11, minor subbands around pH 5-7.5 by agarose isoelectric focusing. The isoenzyme reacted with anti-human brain CK-BB antibodies and formed a hybrid, CK-MB, with CK-MM prepared from healthy human skeletal muscle. The above physicochemical and immunological characteristics of tumor CK-BB were the same as those of normal CK-BB from normal stomach tissue. Optimum pH of tumor CK-BB was more acidic than that of normal CK-BB. Affinity for creatine phosphate and heat sensitivity of tumor CK-BB were slightly lower than those of normal CK-BB. Tumor CK-BB was more stable after iodoacetamide and urea treatments.

• Authors: F Kanemitsu, T Okigaki
• Journal: Clinica chimica acta; international journal of clinical chemistry (Clin Chim Acta) Vol. 151 Issue 1 Pg. 23-31 (Sep 16 1985) ISSN: 0009-8981 [Print] Netherlands
• PMID: 4042368 (Publication Type: Journal Article)

Chemical References

• Isoenzymes
• Urea
• Creatine Kinase
• Iodoacetamide

Topics

• Brain (enzymology)
• Creatine Kinase (metabolism)
• Electrophoresis, Polyacrylamide Gel
• Humans
• Iodoacetamide (pharmacology)
• Isoelectric Focusing
• Isoenzymes (metabolism)
• Molecular Weight
• Muscles (enzymology)
• Stomach (enzymology)
• Stomach Neoplasms (enzymology)
• Thermodynamics
• Urea (pharmacology)