Składanowski A C, Zydowo M M
Department of Biochemistry, Medical School, Gdańsk, Poland.
Acta Biochim Pol. 1988;35(1):29-37.
Two forms of bovine heart AMP deaminase were separated by phosphocellulose column chromatography. Form A with lesser affinity to phosphocellulose exhibited a hyperbolic type of substrate curve and was relatively insensitive to ATP. Form B was strongly activated by 1 mM ATP and its substrate saturation kinetics (without ATP) indicated a cooperative effect. The alteration of adenylate energy charge affected forms A and B differently but within the physiological range, the activity of both forms decreased with the increase in energy charge. The Mr of the two forms was identical as estimated by gel filtration. These activities are compared to those of AMP deaminases from the hearts of other species.
通过磷酸纤维素柱层析分离出两种形式的牛心AMP脱氨酶。对磷酸纤维素亲和力较低的A形式呈现双曲线型底物曲线，且对ATP相对不敏感。B形式被1 mM ATP强烈激活，其底物饱和动力学（无ATP时）显示出协同效应。腺苷酸能荷的改变对A和B两种形式的影响不同，但在生理范围内，两种形式的活性均随能荷增加而降低。通过凝胶过滤估计，这两种形式的相对分子质量相同。将这些活性与其他物种心脏中的AMP脱氨酶活性进行了比较。
