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一种由链霉菌菌株产生的新型人粒细胞弹性蛋白酶抑制剂——弹性蛋白的分离与鉴定

Isolation and characterization of elasnin, a new human granulocyte elastase inhibitor produced by a strain of Streptomyces.

作者信息

Ohno H, Saheki T, Awaya J, Nakagawa A, Omura S

出版信息

J Antibiot (Tokyo). 1978 Nov;31(11):1116-23. doi: 10.7164/antibiotics.31.1116.

Abstract

Elasnin, a new human granulocyte elastase inhibitor, produced by the strain of KM-2753 designated as Streptomyces noboritoensis KM--2753 has been isolated from the fermentation broth by column chromatography on silica gel and neutral alumina. Elasnin is a neutral, colorless, and viscous oil (ND17 = 1.4983, [alpha]18D -0.9 degrees, lambdaEtOHmax 291 nm (epsilon, 7,760) having a molecular formula of C24H40O4 (MW 392) as shown by its elemental analysis and mass spectrum. Elasnin markedly inhibits human granulocyte elastase, but it is almost inactive against pancreatic elastase, chymotrypsin, and trypsin. At 1.3 microgram/ml (3.3 X 10(-6) M), elasnin is 50% inhibitory to human elastase, but it causes 50% inhibition of pancreatic elastase at 30.1 microgram/ml (76.8 X 10(-6) M).

摘要

弹性蛋白酶抑制剂(elasnin)是由编号为KM - 2753的诺博里链霉菌(Streptomyces noboritoensis KM - 2753)产生的一种新型人粒细胞弹性蛋白酶抑制剂,已通过硅胶柱色谱和中性氧化铝从发酵液中分离出来。弹性蛋白酶抑制剂是一种中性、无色的粘性油(20℃时折光率为1.4983,旋光度[α]18D -0.9°,乙醇中最大吸收波长λmax 291nm(摩尔吸光系数ε为7760),经元素分析和质谱分析表明其分子式为C24H40O4(分子量392)。弹性蛋白酶抑制剂能显著抑制人粒细胞弹性蛋白酶,但对胰弹性蛋白酶、胰凝乳蛋白酶和胰蛋白酶几乎没有活性。在1.3微克/毫升(3.3×10-6摩尔)时,弹性蛋白酶抑制剂对人弹性蛋白酶有50%的抑制作用,但在30.1微克/毫升(76.8×10-6摩尔)时才能对胰弹性蛋白酶产生50%的抑制作用。

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