FULL ANTITUMOR ACTION OF RECOMBINANT SEMINAL RIBONUCLEASE DEPENDS ON THE REMOVAL OF ITS N-TERMINAL METHIONINE

被引:39
作者
ADINOLFI, BS [1 ]
CAFARO, V [1 ]
DALESSIO, G [1 ]
DIDONATO, A [1 ]
机构
[1] UNIV NAPLES FEDERICO II,DIPARTIMENTO CHIM ORGAN & BIOL,I-80134 NAPLES,ITALY
关键词
D O I
10.1006/bbrc.1995.2163
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1995 Academic Press, Inc.
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收藏
页码:525 / 532
页数:8
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