PURIFICATION AND CHARACTERIZATION OF HUMAN T-CELL LEUKEMIA-VIRUS TYPE-I PROTEASE PRODUCED IN ESCHERICHIA-COLI

被引：26

作者：

KOBAYASHI, M ^{[1
]}

OHI, Y ^{[1
]}

ASANO, T ^{[1
]}

HAYAKAWA, T ^{[1
]}

KATO, K ^{[1
]}

KAKINUMA, A ^{[1
]}

HATANAKA, M ^{[1
]}

机构：

[1] KYOTO UNIV,INST VIRUS RES,KYOTO 606,JAPAN

来源：

FEBS LETTERS | 1991年 / 293卷 / 1-2期

关键词：

HTLV-I PROTEASE; ASPARTIC PROTEASE; GAG PRECURSOR;

D O I：

10.1016/0014-5793(91)81162-2

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：

Human T-cell leukemia virus type I (HTLV-I) protease has been purified to homogeneity from a strain of recombinant Escherichia coli. The protease was expressed as a larger precursor, which was autoprocessed to form a mature protease. Protein chemical analyses revealed the coding sequence of mature protease, which agreed with the putative sequence predicted from the sequence of bovine leukemia virus protease. The purified protease processed the natural substrate gag precursor (p53) to form gag p19 and gag p24. The protease activity was inhibited by pepstatin A. These results provide direct evidence that this protease belongs to the aspartic protease family and has an activity consistent with the protease in HTLV-I virion.

引用

页码：106 / 110

页数：5

共 28 条

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