Murakami S, Harada S, Kojima F, Kinoshita N, Takahashi Y, Hamada M, Takeuchi T, Aoyagi T
Institute of Microbial Chemistry, Tokyo, Japan.
J Enzyme Inhib. 1995;9(4):263-75. doi: 10.3109/14756369509036555.
Belactins A and B, new inhibitors of serine carboxypeptidase were discovered in the fermentation broth of Saccharopolyspora sp. MK19-42F6. They were purified by ethyl acetate extraction, silica gel chromatography, Sephadex LH20 chromatography, Capcellpak C18 SG120 reversed phase HPLC and centrifugal partition chromatography (CPC) following their inhibitory activity against carboxypeptidase Y (CP-Y). The inhibition constants (Ki) of belactins A and B against CP-Y are 0.14 and 0.27 microM respectively. Belactins A and B have highly specific inhibitory activities for CP-Y among various peptidases, have no antimicrobial activities at 100 micrograms/ml and have low toxicities.
在糖多孢菌属菌株MK19 - 42F6的发酵液中发现了丝氨酸羧肽酶的新型抑制剂贝拉汀A和B。根据它们对羧肽酶Y(CP - Y)的抑制活性,通过乙酸乙酯萃取、硅胶柱色谱、葡聚糖凝胶LH20柱色谱、Capcellpak C18 SG120反相高效液相色谱和离心分配色谱(CPC)对其进行纯化。贝拉汀A和B对CP - Y的抑制常数(Ki)分别为0.14和0.27微摩尔。在各种肽酶中,贝拉汀A和B对CP - Y具有高度特异性抑制活性,在100微克/毫升时无抗菌活性且毒性较低。