Spychała J, Kaletha K, Makarewicz W
Biochem J. 1985 Oct 15;231(2):329-33. doi: 10.1042/bj2310329.
The AMP deaminase activity measured in crude chicken liver extract did not change significantly during development. The livers of 10- and 14-day chick embryos, 1-day, 5-, 10- and 16-week-old chickens and adult hens were examined for the existence of multiple forms of AMP deaminase. Phosphocellulose column chromatography revealed the existence of two peaks of enzyme activity in the liver of 10- and 16-week-old chickens and adult hens. Kinetic studies with the preparations of AMP deaminase revealed sigmoid-shaped substrate-saturation curves at all developmental stages and hyperbolic-shaped saturation curves for the enzyme form appearing in 10-week-old chickens. All AMP deaminases investigated were susceptible to activation by ATP and inhibition by Pi. Kinetic and regulatory properties as well as pH optima of all the enzyme preparations tested indicate that AMP deaminase isolated from the embryos and from 1-day-old chicks was similar to the form I isolated from adult hens and differed significantly from the form II of this enzyme.
在粗制鸡肝提取物中测得的AMP脱氨酶活性在发育过程中没有显著变化。对10日龄和14日龄鸡胚、1日龄、5周龄、10周龄和16周龄鸡以及成年母鸡的肝脏进行了检查,以确定是否存在多种形式的AMP脱氨酶。磷酸纤维素柱层析显示,在10周龄和16周龄鸡以及成年母鸡的肝脏中存在两个酶活性峰。对AMP脱氨酶制剂的动力学研究表明,在所有发育阶段底物饱和曲线均为S形,而在10周龄鸡中出现的酶形式的饱和曲线为双曲线形。所有研究的AMP脱氨酶都易受ATP激活和Pi抑制。所有测试酶制剂的动力学和调节特性以及最适pH表明,从胚胎和1日龄雏鸡中分离的AMP脱氨酶与从成年母鸡中分离的I型相似,与该酶的II型有显著差异。