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鸡肝中α - N - 苯甲酰精氨酸 - 2 - 萘酰胺酰胺水解酶活性(作者译)

[alpha-n-benzoylarginine-2-naphthylamide-amidohydrolase activity in chicken liver (author's transl)].

作者信息

Barceló F, Vives N, Bozal J

出版信息

Rev Esp Fisiol. 1980 Sep;36(3):311-20.

PMID:6904059
Abstract

The enzyme activity from chicken liver that hydrolizes alpha-N-benzoil-DL-arginine-2-naphthylamide (BANA) has been separated into three active fractions by chromatography on Sephadex G-100 and DEAE-cellulose. The enzyme in Fraction FEA has a molecular weight greater than or equal to 100,000. The other two enzymes in Fractions FE1B and FE2B have a molecular weight around 23,000 and are separated by DEAE-cellulose chromatography. The BANA-hydrolase of fraction FE2B is unstable at pH alkaline and activates trypsinogen, in contrast with the enzyme of fraction FEB1. Both are thiol enzymes which behave analogously against activators (cysteine, dithiotreitol and 2-mercaptoethanol) and inhibitors (PCMB, IAA, N-ethylmaleimide, Cu2+, Hg2+ and Zn2+).

摘要

通过在葡聚糖凝胶G - 100和二乙氨基乙基纤维素上进行色谱分析,鸡肝中水解α - N - 苯甲酰 - DL - 精氨酸 - 2 - 萘酰胺(BANA)的酶活性已被分离成三个活性部分。FEA部分的酶分子量大于或等于100,000。FE1B和FE2B部分的其他两种酶分子量约为23,000,并通过二乙氨基乙基纤维素色谱法分离。与FEB1部分的酶相比,FE2B部分的BANA水解酶在碱性pH下不稳定,并能激活胰蛋白酶原。两者都是硫醇酶,对激活剂(半胱氨酸、二硫苏糖醇和2 - 巯基乙醇)和抑制剂(对氯汞苯甲酸、吲哚 - 3 - 乙酸、N - 乙基马来酰亚胺、Cu2 +、Hg2 +和Zn2 +)表现出类似的行为。

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