Back to Search
Start Over
Some biochemical characteristics of a partially purified extracellular keratinase from trichophyton schoenleinii
- Source :
- Zentralblatt für Bakteriologie. 277:236-244
- Publication Year :
- 1992
- Publisher :
- Elsevier BV, 1992.
-
Abstract
- A Trichophyton schoenleinii (T. schoenleinii) strain from tinea favus was cultured in a liquid medium, from which an extracellular keratinase extract was obtained. The keratinase was partially purified with carboxymethyl-cellulose (CMC) column chromatography. Some biochemical characteristics of the keratinase were then examined. Its molecular weight was estimated to be 38,000 on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). The optimal temperature was 50 degrees C, and the optimal pH value was 5.5. The keratinolytic activity was specifically increased by Fe++ and Fe .
- Subjects :
- Sodium
Guinea Pigs
Immunology
chemistry.chemical_element
medicine.disease_cause
Substrate Specificity
Column chromatography
Trichophyton
medicine
Extracellular
Animals
Humans
chemistry.chemical_classification
Gel electrophoresis
biology
biology.organism_classification
Enzyme
chemistry
Biochemistry
Keratinase
Dermatophyte
biology.protein
Keratins
Hair
Peptide Hydrolases
Subjects
Details
- ISSN :
- 09348840
- Volume :
- 277
- Database :
- OpenAIRE
- Journal :
- Zentralblatt für Bakteriologie
- Accession number :
- edsair.doi.dedup.....c70f05e46127ff0b60ea75bb25ae62d4
- Full Text :
- https://doi.org/10.1016/s0934-8840(11)80618-3