Human senile cataractous lens protease. Isolation and some chemical characteristics
- 1 November 1971
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 125 (2), 575-584
- https://doi.org/10.1042/bj1250575
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.Keywords
This publication has 18 references indexed in Scilit:
- Histochemical identification of lysosomal enzymes in lens epithelial cellsExperimental Eye Research, 1967
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964
- Aminopeptidase of the ocular lens I. Metal-ion requirements and synergistic activationBiochimica et Biophysica Acta, 1963
- LENS AMINOPEPTIDASE .1. PURIFICATION AND PROPERTIES1963
- LENS AMINOPEPTIDASE .2. HYDROLYSIS OF POLYPEPTIDES1963
- Neutral proteinases in the lensBiochemical Journal, 1962
- The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects and patients with cancer and other diseasesCancer, 1958
- A spectrophotometric determination of trypsin and chymotrypsinBiochimica et Biophysica Acta, 1955
- A MODIFIED NINHYDRIN REAGENT FOR THE PHOTOMETRIC DETERMINATION OF AMINO ACIDS AND RELATED COMPOUNDSJournal of Biological Chemistry, 1954
- Influence of Microwaves on Certain Enzyme Systems in the Lens of the Eye*American Journal of Ophthalmology, 1951