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Human liver cathepsin D. Purification, crystallization and preliminary X-ray diffraction analysis of a lysosomal enzyme.

Abstract：

:The two-chain form of active cathepsin D, a glycosylated, lysosomal aspartic proteinase, has been isolated from human liver. Isoelectric focusing revealed two major species of enzyme that differed by approximately 0.2 pI unit. Crystals suitable for X-ray diffraction analysis were prepared from acidic solutions using precipitation with ammonium sulfate. The hexagonal crystals diffracted X-rays to beyond 3.1 A resolution and belonged to space group P6(1) (or P6(5)) with cell constants a = b = 125.9 A, c = 104.1 A, gamma = 120.0 degrees. The crystals likely contain two molecules in the asymmetric unit, giving a solvent content of 56% (v/w). Biochemical analysis of crystals indicated that both isoforms were present in approximately equimolar proportions. Full structure determination of the enzyme is underway.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Gulnik S,Baldwin ET,Tarasova N,Erickson J

doi

10.1016/0022-2836(92)90696-h

keywords:

subject

Has Abstract

pub_date

1992-09-05 00:00:00

pages

265-70

issue

1

eissn

0022-2836

issn

1089-8638

pii

0022-2836(92)90696-H

journal_volume

227

pub_type

杂志文章

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