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重组精液核糖核酸酶的完全抗肿瘤作用取决于其N端甲硫氨酸的去除。

Full antitumor action of recombinant seminal ribonuclease depends on the removal of its N-terminal methionine.

作者信息

Adinolfi B S, Cafaro V, D'Alessio G, Di Donato A

机构信息

Dipartimento di Chimica Organica e Biologica, Università di Napoli Federico II, Italy.

出版信息

Biochem Biophys Res Commun. 1995 Aug 15;213(2):525-32. doi: 10.1006/bbrc.1995.2163.

Abstract

Bovine seminal RNase (BS-RNase) is a dimeric member of the pancreatic-like ribonuclease superfamily, with antitumor activity. We report here that recombinant Met(-1) BS-RNase is a less potent cytotoxic factor, while structurally and catalytically indistinguishable from BS-RNase isolated from natural sources. Mature recombinant BS-RNase instead displays full antitumor action. This suggests that the conformation of the N-terminal region of BS-RNase is among the structural determinants of its antitumor action, in addition to its catalytic activity and its quaternary structure.

摘要

牛精浆核糖核酸酶(BS-RNase)是胰样核糖核酸酶超家族的二聚体成员,具有抗肿瘤活性。我们在此报告,重组Met(-1) BS-RNase是一种活性较弱的细胞毒性因子,但其结构和催化活性与从天然来源分离的BS-RNase并无差异。相反,成熟的重组BS-RNase具有完全的抗肿瘤作用。这表明,除了其催化活性和四级结构外,BS-RNase N端区域的构象也是其抗肿瘤作用的结构决定因素之一。

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