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Literature DB >> 5144759

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

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.

Entities: Chemical Disease Species

Mesh：

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Year: 1971 PMID： 5144759 PMCID： PMC1178095 DOI： 10.1042/bj1250575

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

18 in total

1. AMINOPEPTIDASE OF THE OCULAR LENS. I. METAL-ION REQUIREMENTS AND SYNERGISTIC ACTIVATION.

Authors: J B WOLFF; R A RESNIK
Journal: Biochim Biophys Acta Date: 1963-08-06

2. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.

Authors: B J DAVIS
Journal: Ann N Y Acad Sci Date: 1964-12-28 Impact factor: 5.691

3. A spectrophotometric determination of trypsin and chymotrypsin.

Authors: G W SCHWERT; Y TAKENAKA
Journal: Biochim Biophys Acta Date: 1955-04

4. Neutral proteinases in the lens.

Authors: S G WALEY; R VAN HEYNINGEN
Journal: Biochem J Date: 1962-05 Impact factor: 3.857

5. Lens aminopeptidase. I. Purification and properties.

Authors: A SPECTOR
Journal: J Biol Chem Date: 1963-04 Impact factor: 5.157

6. Lens aminopeptidase. II. Hydrolysis of polypeptides.

Authors: A SPECTOR; C MECHANIC
Journal: J Biol Chem Date: 1963-07 Impact factor: 5.157

7. The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects and patients with cancer and other diseases.

Authors: J A GOLDBARG; A M RUTENBURG
Journal: Cancer Date: 1958 Mar-Apr Impact factor: 6.860

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

1. AMINOPEPTIDASE OF THE OCULAR LENS. I. METAL-ION REQUIREMENTS AND SYNERGISTIC ACTIVATION.

2. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.

3. A spectrophotometric determination of trypsin and chymotrypsin.

4. Neutral proteinases in the lens.

5. Lens aminopeptidase. I. Purification and properties.

6. Lens aminopeptidase. II. Hydrolysis of polypeptides.

7. The colorimetric determination of leucine aminopeptidase in urine and serum of normal subjects and patients with cancer and other diseases.

8. A modified ninhydrin reagent for the photometric determination of amino acids and related compounds.

9. Influence of microwaves on certain enzyme systems in the lens of the eye.

10. Histochemical inentification of lysosomal enzymes in lens epithelial cells.

1. Age-related changes in the proteolytic enzymes of mammalian lens.

2. Metalloproteases of human articular cartilage that digest cartilage proteoglycan at neutral and acid pH.

3. Metal-dependent proteinase of the lens. Assay, purification and properties of the bovine enzyme.