PURIFICATION AND SOME REGULATORY PROPERTIES OF HUMAN-HEART ADENYLATE DEAMINASE

被引：25

作者：

KALETHA, K ^{[1
]}

SKLADANOWSKI, A ^{[1
]}

BOGDANOWICZ, S ^{[1
]}

ZYDOWO, M ^{[1
]}

机构：

[1] DEBRECEN UNIV MED,SCH MED,DEPT PHYSIOL,H-4012 DEBRECEN,HUNGARY

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY | 1979年 / 10卷 / 11期

关键词：

D O I：

10.1016/0020-711X(79)90125-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. 1. Adenylate deaminase (EC 3.5.4.6) was purified from human heart by chromatography on cellulose phosphate. 2. 2. The enzyme shows sigmoid-shaped kinetics in the presence of 100 mM potassium chloride with the K0.5 (the substrate concentration required to reach half-maximum velocity) of 6mM. 3. 3. On addition of ATP the kinetics are transformed to hyperbolic, the K0.5 value decreases and maximum velocity increases. Orthophosphate was shown to be a negative effector of human heart adenylate deaminase, changing both K0.5 and Vmax values. 4. 4. The influence of temperature on the enzyme kinetics was investigated, from which activation energy (Ea) and the heat of enzyme-substrate complex formation (ΔHs) was calculated. 5. 5. It is concluded that human heart adenylate deaminase is an enzyme of mixed (Km, Vmax-type) type of regulation. © 1979.

引用

页码：925 / 929

页数：5

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