ArticleBiochemistry and biophysics reports2020
A simple purification procedure of buffalo lung cathepsin H, its properties and influence of buffer constituents on the enzyme activity.
Article in Biochemistry and biophysics reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Cathepsin H as a causal risk factor and therapeutic target in proliferative diabetic retinopathy.Journal of translational medicine · 2026Article
- Characterization of alkaline protease enzyme produced from marine yeast Candida orthopsilosis AKB-1 and its applications.Folia microbiologica · 2025Article
- Investigation of anticancer potential of a novel bioactive molecule from Trichosporon asahii VITSTB1 in breast cancer cell lines: an in vitro study.Medical oncology (Northwood, London, England) · 2024Article
- Unraveling anticancer potential of a novel serine protease inhibitor from marine yeast Candida parapsilosis ABS1 against colorectal and breast cancer cells.World journal of microbiology & biotechnology · 2023Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundCathepsin 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.
methodsPurification 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.
resultsThe SDS-PAGE result showed buffalo cathepsin H to be a single-chain molecule having MW, NH
conclusionCatheptic activity was found to be quite stable at least for 20-30 min between pH 4.5-7.0, buffer concentration of 1 × 10 GENERAL SIGNIFICANCE: This study seems to provide valuable information regarding the biochemistry of cathepsin H in general as well as influence of buffer constituents on enzyme activity and physiological role in particular.
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