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M94A3286.TXT
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1994-10-25
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Document 3286
DOCN M94A3286
TI The cytoskeletal proteins cleaving activity of the recombinant HIV-1
protease.
DT 9412
AU Azuma R; Furuishi K; Saito A; Shinagawa H; Ikeda S; Shoji S; Dept. of
Biochem., Fac. of Pharm. Sci., Kumamoto Univ., Japan.
SO Int Conf AIDS. 1994 Aug 7-12;10(1):110 (abstract no. PA0059). Unique
Identifier : AIDSLINE ICA10/94369289
AB OBJECTIVE: The purpose of the present work was to isolate a HIV-1
protease from HIV-1 protease expressing E. coli, and to determine its
enzymatic activity for synthetic oligopeptides and nonviral protein
substrates. METHODS: HIV-1 protease expressing E. coli was lysed,
extracted, and partially purified by DEAE-Cellulofine and SP-Toyopearl
column chromatography. The enzymatic cleaving activities for synthetic
oligopeptides and proteins were determined by HPLC and SDS-PAGE,
respectively. RESULTS AND DISCUSSION: The HIV-1 protease was separated
from the HIV-1 protease expressing E. coli. It cleaved the Tyr-Pro bond
of the various oligopeptides, and had a pH optimum at pH 5.5 for
suc-Ser-Gln-Asn-Tyr-Pro-Ile-Val-Gln. It was strongly inhibited by
pepstatin A. The enzyme specifically hydrolyzed a Phe-Ala bond of
alpha-actinin which is a component of cytoskeltal proteins. The enzyme
may be important for penetration of the virus into the host cells in
addition to the key enzyme in HIV-1 gag protein processing.
DE Amino Acid Sequence Binding Sites Cytoskeletal
Proteins/GENETICS/*METABOLISM Escherichia coli/GENETICS Human
Hydrogen-Ion Concentration HIV Protease/GENETICS/*METABOLISM
HIV-1/*ENZYMOLOGY/GENETICS In Vitro Molecular Sequence Data
Oligopeptides/CHEMICAL SYNTHESIS/GENETICS/METABOLISM Recombinant
Proteins/GENETICS/METABOLISM Substrate Specificity MEETING ABSTRACT
SOURCE: National Library of Medicine. NOTICE: This material may be
protected by Copyright Law (Title 17, U.S.Code).