Human senile cataractous lens protease. Isolation and some chemical characteristics-Reference-Cited by-同舟云学术

Human senile cataractous lens protease. Isolation and some chemical characteristics

Published:1971-11-01 Issue:2 Volume:125 Page:575-584
ISSN:0306-3283
Container-title:Biochemical Journal
language:en
Short-container-title:

Author:

Swanson Arnold A.¹,Nichols John T.¹

Affiliation:

1. Department of Biochemistry, Medical University of South Carolina, Charleston, S.C. 29401, U.S.A.

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.

Publisher

Portland Press Ltd.

Link

https://portlandpress.com/biochemj/article-pdf/125/2/575/774190/bj1250575.pdf

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