Cobalt-activated acylase and aminoacylase I in human malignant tumors.

Abstract

The activities and isoenzyme pattern of cobalt-activated acylase and of aminoacylase I were estimated in carcinomas of bronchi, lung, thorax, stomach, colon and uterus. In all cancer tissues the activity of cobalt-activated acylase was markedly increased as compared with the normal tissue. Alterations of the isoenzyme pattern of cobalt-activated acylase were found in the carcinoma of stomach and of uterus, with the increased expression of the form-1 of the enzyme. No regularity in the aminoacylase I changes in tumor tissues has been observed.

• Authors: W Tyran, M Jeleń, J Kołodziej
• Journal: Neoplasma (Neoplasma) Vol. 27 Issue 3 Pg. 317-20 ( 1980) ISSN: 0028-2685 [Print] Slovakia
• PMID: 7453852 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Glutamates
• Isoenzymes
• Cobalt
• Aminopeptidases
• Amidohydrolases
• aminoacylase I

Topics

• Amidohydrolases (analysis)
• Aminopeptidases (analysis)
• Breast Neoplasms (enzymology)
• Cobalt (pharmacology)
• Colonic Neoplasms (enzymology)
• Enzyme Activation
• Female
• Glutamates (analysis)
• Humans
• Isoenzymes (analysis)
• Lung Neoplasms (enzymology)
• Neoplasms (enzymology)
• Stomach Neoplasms (enzymology)