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. 1967 Aug;104(2):601–608. doi: 10.1042/bj1040601

Lysosomal acid proteinase of rabbit liver

A J Barrett 1
PMCID: PMC1270626  PMID: 6058110

Abstract

1. Acid proteinase from rabbit liver lysosomes was purified about 1000-fold, on a protein basis. 2. The purification procedure involved isolation of a lysosomal–mitochondrial pellet and conversion of this into an acetone-dried powder. 3. The enzyme was extracted with an acidic buffer and subjected to column chromatography with DEAE-Sephadex and Sephadex G-100. 4. The molecular weight of the enzyme was 50000–52000. 5. Maximal activity against haemoglobin was obtained at pH3·2; serum albumin was attacked, but very much more slowly. 6. Several possible inhibitors of the enzyme were tested. Thiol-blocking reagents, several inhibitors of trypsin and chymotrypsin, and a chelating agent were without effect. 7. The enzyme was competitively inhibited by 3-phenylpyruvic acid at low concentrations. 8. Dithiothreitol caused rapid inactivation of the enzyme at pH8. 9. It is concluded that this enzyme is a form of cathepsin D, which may be widely distributed in lysosomes.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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