多磷酸肌醇与AMP脱氨酶的相互作用。

The interaction of polyphosphoinositols with AMP deaminase.

作者信息

Spychała J

机构信息

Department of Biochemistry, Academic Medical School, Gdańsk, Poland.

出版信息

Biochem Biophys Res Commun. 1987 Oct 14;148(1):106-11. doi: 10.1016/0006-291x(87)91082-5.

DOI:10.1016/0006-291x(87)91082-5

PMID:2823797

Abstract

Polyphosphoinositols coupled to epoxy-activated Sepharose retained chicken liver AMP deaminase in a similar manner as phosphocellulose. After elution from polyphosphoinositol-Sepharose, in contrast to inositol-Sepharose and phosphocellulose, low Km AMP deaminase from the chicken liver exhibited markedly elevated S0.5 value. Several commercially available polyphosphoinositols were tested with rat liver AMP deaminase and only 1,3,4,5 IP4 was found to stimulate the enzyme. This is the first report on the effect of naturally occurring polyphosphoinositol derivative on the soluble enzyme.

摘要

与环氧活化琼脂糖偶联的多磷酸肌醇保留鸡肝AMP脱氨酶的方式与磷酸纤维素相似。从多磷酸肌醇-琼脂糖洗脱后，与肌醇-琼脂糖和磷酸纤维素不同，鸡肝的低Km AMP脱氨酶表现出显著升高的S0.5值。用大鼠肝AMP脱氨酶测试了几种市售的多磷酸肌醇，发现只有1,3,4,5-IP4能刺激该酶。这是关于天然存在的多磷酸肌醇衍生物对可溶性酶作用的首次报道。