Faculty of Pharmaceutical Sciences, Science University of Tokyo, Shinjuku-ku, Tokyo 162, Japan.
Plant Physiol. 1979 Mar;63(3):562-6. doi: 10.1104/pp.63.3.562.
Inhibitory activity directed against metalloenzymes has been highly purified from extracts of red kidney beans (Phaseolus vulgaris). The inhibitor is a substance of small molecular weight and appears to be a chelator of Zn(2+). One milligram of the preparation inhibited 23 milligrams carboxypeptidase A. The inhibitor also strongly inhibited carboxypeptidase B and alkaline phosphatase and could activate phosphoglucomutase that had previously been inactivated with Zn(2+). The isoelectric point of the inhibitor is 4.7. The inhibitor activity was abolished by preincubation with Zn(2+), Ni(2+), Co(2+), or Cu(2+). The mechanism of inhibition of carboxypeptidases and alkaline phosphatase by the bean inhibitor is apparently due to the complexing and complete removal of Zn(2+) from the enzymes.
从红芸豆（菜豆属植物）提取物中高度纯化出了一种针对金属酶的抑制活性物质。该抑制剂是一种小分子物质，似乎是 Zn(2+) 的螯合剂。一毫克该制剂可抑制 23 毫克的羧肽酶 A。该抑制剂还强烈抑制羧肽酶 B 和碱性磷酸酶，并可激活先前已被 Zn(2+) 失活的磷酸葡萄糖变位酶。抑制剂的等电点为 4.7。抑制剂活性在与 Zn(2+)、Ni(2+)、Co(2+) 或 Cu(2+) 预孵育后被消除。该豆类抑制剂对羧肽酶和碱性磷酸酶的抑制机制显然是由于 Zn(2+) 与酶的络合和完全去除。
