A simple purification procedure of buffalo lung cathepsin H, its properties and influence of buffer constituents on the enzyme activity.

ABSTRACT:

Background

Cathepsin H (E.C.3.4.22.16) belongs to a family of lysosomal cysteine protease which regulates diverse normal biological processes mainly in intracellular proteolysis.

Methods

Purification of cathepsin H from an unstudied system i.e. buffalo lung has been achieved by a simple process developed after incorporating appropriate alteration in the available methods for isolation of the enzyme from other sources. The use of DEAE-Cellulose and SP-Sephadex C-50 helped in better and simultaneous separation of cathepsin B and H up to homogeneity.

Results

The SDS-PAGE result showed buffalo cathepsin H to be a single-chain molecule having MW, NH₂- and COOH- terminal residues of 25.4 kDa, Lys and Val respectively. The enzyme was a glycoprotein with pI of 6.2;

SUBMITTER: Singh S 

PROVIDER: S-EPMC7013249 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature