Affinity purification of the HIV-1 protease
作者： Jill C. Heimbach , Victor M. Garsky , Stuart R. Michelson , Richard A.F. Dixon , Irving S. Sigal
DOI: 10.1016/0006-291X(89)91762-2
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摘要: Abstract An inhibitor of the HIV-1 protease has been employed in generation a resin which allows rapid purification this enzyme. A peptide substrate analogue, H 2 N-Ser-Gln-Asn-(Phe-Ψ[CH N]-Pro)-Ile-Val-Gln-OH, was coupled to agarose resin. The expressed E. coli and supernatant from lysed cells passed through affinity Active then eluted with buffer change pH 10 M NaCl. Final homogeneous preparation, capable crystallization, achieved hydrophobic interaction chromatography. Solutions containing bound competitive inhibitors do not bind column.
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