大鼠心脏中的5'-核苷酸酶。存在两种具有不同底物特异性的可溶性酶的证据。
5'-Nucleotidases in rat heart. Evidence for the occurrence of two soluble enzymes with different substrate specificities.
作者信息
Truong V L, Collinson A R, Lowenstein J M
机构信息
Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.
出版信息
Biochem J. 1988 Jul 1;253(1):117-21. doi: 10.1042/bj2530117.
Abstract
Chromatography of soluble proteins from rat heart on phosphocellulose columns separates two 5'-nucleotidases. The first to emerge from the column shows a preference for AMP over IMP as substrate, whereas the second shows a preference for IMP over AMP. The properties of the IMP-preferring enzyme, including the conditions under which it is eluted from phosphocellulose columns, show it to be the enzyme studied by Itoh, Oka & Ozasa [Biochem. J. (1986) 235, 847-851]. The kinetic properties of the AMP-preferring enzyme indicate that it is likely to be the enzyme responsible for the production of adenosine under conditions of hypoxia and increased work load, and with metabolic stresses such as a high load of acetate.
摘要
用磷酸纤维素柱对大鼠心脏的可溶性蛋白质进行色谱分析，可分离出两种5'-核苷酸酶。首先从柱中洗脱出来的酶对AMP作为底物的偏好高于IMP，而第二种酶对IMP作为底物的偏好高于AMP。偏好IMP的酶的特性，包括其从磷酸纤维素柱上洗脱的条件，表明它就是Itoh、Oka和Ozasa [《生物化学杂志》(1986年)235卷，847 - 851页]所研究的酶。偏好AMP的酶的动力学特性表明，在缺氧、工作负荷增加以及存在代谢应激（如高负荷乙酸盐）的情况下，它可能是负责生成腺苷的酶。
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