Abnormalities of cobalt-activated acylase from human sarcoma, carcinoma and the adjacent tissue.

Abstract

Cobalt-activated acylase form-2 from human uterine myosarcoma, lung adenocarcinoma and the adjacent tissue was isolated, purified and characterized. It was found, that the enzyme from the malignant neoplasms differed both from the normal tissue and benign tumor acylase-2 in its Km value, temperature optimum and effect of some ions. Some abnormal properties (pH dependence, activation by cobalt and thermostability) were common for benign and malignant tumors. In lung tissue adjacent to adenocarcinoma, some deviations of acylase properties were observed, similar to that found in tumor, indicating that biochemical changes may be present also in tissues unaffected by the neoplastic growth by the histopathological criteria.

• Authors: W Tyran, M Ujec, K Stasiak, J Kwiatkowska
• Journal: Archivum immunologiae et therapiae experimentalis (Arch Immunol Ther Exp (Warsz)) Vol. 31 Issue 4 Pg. 565-74 ( 1983) ISSN: 0004-069X [Print] Switzerland
• PMID: 6422903 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Cobalt
• Edetic Acid
• Amidohydrolases
• amidase
• cobaltous chloride

Topics

• Adenocarcinoma (enzymology)
• Amidohydrolases (antagonists & inhibitors, isolation & purification, metabolism)
• Cobalt (pharmacology)
• Drug Stability
• Edetic Acid (pharmacology)
• Enzyme Activation
• Female
• Humans
• Lung Neoplasms (enzymology)
• Myosarcoma (enzymology)
• Temperature
• Uterine Neoplasms (enzymology)