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PMID: 5144759 Published · ppublish English Journal Article

Human senile cataractous lens protease. Isolation and some chemical characteristics.

The Biochemical journal ·Vol. 125 ·No. 2 ·1971-11-00 ·Pages 575-84

Swanson AA, Nichols JT

Abstract

A proteolytic enzyme was isolated from human senile cataractous lens by anion-exchange and gel-filtration chromatography. Sedimentation and zone-electrophoretic experiments indicated a high degree of homogeneity for the enzyme. A molecular weight of 27000 was calculated from measurements of sedimentation velocity and diffusion coefficient. Chelating agents decreased activity which could be restored by addition of certain bivalent metal ions. Di-isopropyl phosphorofluoridate and phenylmethanesulphonyl fluoride inhibit the proteolytic activities. Optimum rates of hydrolysis were observed at pH5.2.

MeSH Terms
Aged Amino Acids/analysis Cataract/enzymology Chromatography, Gel Chromatography, Ion Exchange Cobalt Diffusion Electrophoresis, Disc Fluorides Humans Hydrogen-Ion Concentration Isoflurophate Lens, Crystalline/enzymology Manganese Molecular Weight Nickel Peptide Hydrolases/analysis,isolation & purification Protease Inhibitors Temperature Ultracentrifugation
Chemicals
Amino Acids Protease Inhibitors Isoflurophate Cobalt Manganese Nickel Peptide Hydrolases Fluorides
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Swanson A A
Nichols J T
References (18)
18 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1250575
Published
1971-11-00
Pages
575-84
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1178095
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1250575 PMC Full Text View journal details
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