IDENTIFICATION OF GUANYLATE CYCLASE ACTIVITY FROM ARTERIA CORONARIA OF CATTLE

  • 1 January 1976
    • journal article
    • research article
    • Vol. 35  (12) , 1595-1601
Abstract
Guanylate cyclase activities were identified in a soluble fraction and a particulate fraction obtained from the coronary arteries of cattle. The Km value was 1.0 .+-. 0.7 .cntdot. 10-4 M for the enzyme substrate complex of the guanylate cyclase of the soluble fraction and 9.2 .+-. 1.5 .cntdot. 10-4 M for the particulate fraction. For the enzyme activity of the soluble fraction Mn2+ could not be replaced by Ca2+ or Mg2+, whereas for the enzyme activity of the particulate fraction Mn2+ could be replaced by Mg2+ but not by Ca2+. The guanylate cyclase of the particulate fraction was activated by acetylcholine. This activation was cancelled by atropine. Acetylcholine exerts no influence on the guanylate cyclase activity of the soluble fraction. ATP inhibits the enzyme activities of both fractions whereas c[cyclic]AMP shows no influence on the guanylate cyclase activity.

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