淀粉磷酸化酶抑制剂是β-淀粉酶。

Starch Phosphorylase Inhibitor Is beta-Amylase.

机构信息

Department of Agricultural Chemistry, National Taiwan University, Taipei, Taiwan 10764, ROC.

出版信息

Plant Physiol. 1988 Dec;88(4):1154-6. doi: 10.1104/pp.88.4.1154.

DOI:10.1104/pp.88.4.1154

PMID:16666436

原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1055732/

Abstract

The proteinaceous noncompetitive inhibitor of starch phosphorylase isolated from the root of sweet potato (Ipomoea batatas [L.] Lam.) (TC Chang, JC Su 1986 Plant Physiol 80: 534-538) has been identified as a beta-amylase. The starch phosphorylase inhibitor and beta-amylase activities copurified to give a protein indistinguishable from commercial beta-amylase by electrophoretic and immunological methods, and the two activities showed parallel responses in pH, temperature, and inhibitor sensitivity tests. The amylolytic pattern of the inhibitor corresponded to that of beta-amylase and its inhibitory effect toward starch phosphorylase was due to neither deprivation of starch, the primer for the phosphorylase assay, nor the inhibitory effect of amylolytic products.

摘要

从甘薯（Ipomoea batatas [L.] Lam.）根部分离出的淀粉磷酸化酶的蛋白质非竞争性抑制剂（TC Chang，JC Su 1986 Plant Physiol 80: 534-538）已被鉴定为β-淀粉酶。淀粉磷酸化酶抑制剂和β-淀粉酶活性共同纯化，通过电泳和免疫方法得到与商业β-淀粉酶无法区分的蛋白质，并且两种活性在 pH、温度和抑制剂敏感性测试中表现出平行反应。抑制剂的淀粉水解模式与β-淀粉酶相对应，其对淀粉磷酸化酶的抑制作用既不是由于缺乏淀粉（磷酸化酶测定的引物），也不是由于淀粉水解产物的抑制作用。