Busse E
Acta Biol Med Ger. 1976;35(12):1595-601.
Guanylate cyclase activities were identified in a soluble fraction and a particular fraction obtained from the Arteria coronaria of cattle. The Km-value was 1.0 +/- 0.7 - 10(-4) M for the enzyme substrate complex of the guanylate cyclase of the soluble fraction and 9.2 +/- 1.5 - 10(-4) M for the particular fraction. For the enzyme activity of the soluble fraction Mn++ cannot be replaced by Ca++ or Mg++, whereas for the enzyme activity of the particulate fraction Mn++ can be replaced by Mg++ but not by Ca++. The guanylate cyclase of the particulate fraction can be activated by acetylcholine. This activation can be 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 cAMP shows no influence on the guanylate cyclase activity.
在从牛冠状动脉获得的可溶性部分和特定部分中鉴定出鸟苷酸环化酶活性。可溶性部分的鸟苷酸环化酶的酶底物复合物的Km值为1.0±0.7×10⁻⁴M,特定部分的Km值为9.2±1.5×10⁻⁴M。对于可溶性部分的酶活性,Mn²⁺不能被Ca²⁺或Mg²⁺替代,而对于颗粒部分的酶活性,Mn²⁺可以被Mg²⁺替代,但不能被Ca²⁺替代。颗粒部分的鸟苷酸环化酶可被乙酰胆碱激活。这种激活可被阿托品消除。乙酰胆碱对可溶性部分的鸟苷酸环化酶活性没有影响。ATP抑制两个部分的酶活性,而cAMP对鸟苷酸环化酶活性没有影响。