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Affinity purification of HIV-1 and HIV-2 proteases from recombinant E. coli strains using pepstatin-agarose.

Abstract：

:A procedure is described which employs pepstatin-agarose for the affinity purification of either HIV-1 or HIV-2 protease from two similar recombinant E. coli constructs that were developed for the expression of these enzymes. HIV-2 protease was routinely expressed at much higher levels than the HIV-1 enzyme and pepstatin-agarose was the only chromatography step required to isolate pure HIV-2 protease from crude bacterial lysates. A Mono S ionic exchange step following pepstatin-agarose chromatography was sufficient to bring the HIV-1 protease to homogeneity. Purification of either enzyme can be completed in several days yielding homogeneous preparations suitable for crystallization and other physical characterization.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Rittenhouse J,Turon MC,Helfrich RJ,Albrecht KS,Weigl D,Simmer RL,Mordini F,Erickson J,Kohlbrenner WE

doi

10.1016/0006-291x(90)91356-w

subject

Has Abstract

pub_date

1990-08-31 00:00:00

pages

60-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(90)91356-W

journal_volume

171

pub_type

杂志文章

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