Ecto-enzymes of Mammary Gland and Its Tumours. Ca2+- or Mg2+-stimulated Adenosine Triphosphatase and Its Perturbation by Concanavalin A

Overview

Journal Biochem J

Specialty Biochemistry

Date 1980 Oct 1

PMID 6258585

Citations 5

Authors

C A Carraway

F J Corrado 4th

D D Fogle

K L Carraway

Affiliations

Soon will be listed here.

Abstract

Intact viable 13762 mammary-adenocarcinoma ascites cells hydrolyse added ATP. The localization of hydrolysis product and inactivation by the slowly penetrating chemical reagent diazotized sulphanilic acid indicate that this ATPase is at the external surface of the cell. A number of features differentiate this enzyme from mitochondrial, myosin and cation-transport ATPases. It is stimulated by either Ca2+ or Mg2+ and has little or no activity in their absence. It is insensitive to ouabain, oligomycin and azide. It is the major ATPase activity found in homogenates of gently disrupted 13762 cels. The ATPase activity is inhibited at high substrate concentrations and shows an apparent stimulation by concanavalin A in isolated membranes, but not in intact cells. The stimulation by concanavalin A results predominantly from a release from substrate inhibition.

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