家蚕中的腺苷酸环化酶。蛹脂肪体中该酶的性质。

Adenylate cyclase in silkworm. Properties of the enzyme in pupal fat body.

作者信息

Morishima I

出版信息

J Biochem. 1978 Dec;84(6):1495-500. doi: 10.1093/oxfordjournals.jbchem.a132273.

DOI:10.1093/oxfordjournals.jbchem.a132273

Abstract

Adenylate cyclase was assayed in a sonicated preparation of silkworm pupal fat body. The adenylate cyclase was found mostly in the particulate fraction. The activity depended upon either Mg2+ or Mn2+, and the degree of stimulation by Mn2+ was 2 times greater than that by Mg2+ compared at the saturating concentrations. In the presence of Mg2+, the enzyme was inhibited by both EGTA and high concentrations of Ca2+, showing biphasical response to Ca2+. The enzyme was stimulated several-fold by NaF. The enzyme exhibited typical Michaelis-Menten kinetics and Km values were 0.13 mM for MgATP and 0.086 mM for MnATP.

摘要

在家蚕蛹脂肪体的超声破碎制剂中测定了腺苷酸环化酶。腺苷酸环化酶大多存在于颗粒部分。该活性依赖于Mg2+或Mn2+，在饱和浓度下比较，Mn2+的刺激程度比Mg2+大2倍。在Mg2+存在的情况下，该酶受到EGTA和高浓度Ca2+的抑制，对Ca2+表现出双相反应。该酶被NaF刺激了几倍。该酶表现出典型的米氏动力学，MgATP的Km值为0.13 mM，MnATP的Km值为0.086 mM。