Starch phosphorylase inhibitor is β-amylase
Starch phosphorylase inhibitor is β-amylase
复制标题
淀粉磷酸化酶抑制剂是β-淀粉酶
DOI：
10.1104/pp.88.4.1154
复制
发表时间：
1988
期刊：
影响因子：
--
通讯作者：
J. Su
中科院分区：
文献类型：
--
作者：
S. Pan;T. Chang;R. Juang;J. Su
从甘薯根（Ipomoea batatas [L.] Lam.）分离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。通过电泳和免疫学方法，淀粉磷酸化酶抑制剂和β-淀粉酶活性共纯化得到与商业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响应。该抑制剂的淀粉分解模式与β-淀粉酶的淀粉分解模式相对应，其对淀粉磷酸化酶的抑制作用既不是由于磷酸化酶测定引物淀粉的缺乏，也不是淀粉分解产物的抑制作用。
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 β-amylase. The starch phosphorylase inhibitor and β-amylase activities copurified to give a protein indistinguishable from commercial β-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 β-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.