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Insight into the collagen-degrading activity of a serine protease in the latex of Ficus carica cultivar Masui Dauphine
- Source :
- Bioscience, Biotechnology, and Biochemistry. 85:1147-1156
- Publication Year :
- 2021
- Publisher :
- Informa UK Limited, 2021.
-
Abstract
- Ficus carica produces, in addition to the cysteine protease ficin, a serine protease. Earlier study on a serine protease from F. carica cultivar Brown Turkey showed that it specifically degraded collagen. In this study, we characterized the collagenolytic activity of a serine protease in the latex of F. carica cultivar Masui Dauphine. The serine protease degraded denatured, but not undenatured, acid-solubilized type I collagen. It also degraded bovine serum albumin, while the collagenase from Clostridium histolyticum did not. These results indicated that the serine protease in Masui Dauphine is not collagen-specific. The protease was purified to homogeneity by two-dimensional gel electrophoresis, and its partial amino acid sequence was determined by liquid chromatography-tandem mass spectrometry. BLAST searches against the Viridiplantae (green plants) genome database revealed that the serine protease was a subtilisin-like protease. Our results contrast with the results of the earlier study stating that the serine protease from F. carica is collagen-specific.
- Subjects :
- Protein Denaturation
Hot Temperature
Latex
medicine.medical_treatment
Gene Expression
Applied Microbiology and Biotechnology
Biochemistry
Substrate Specificity
Analytical Chemistry
Clostridium histolyticum
medicine
Animals
Electrophoresis, Gel, Two-Dimensional
Amino Acid Sequence
Subtilisins
Bovine serum albumin
Molecular Biology
Plant Proteins
Gel electrophoresis
Serine protease
Protease
Sequence Homology, Amino Acid
biology
Plant Extracts
Chemistry
Organic Chemistry
General Medicine
Ficus
biology.organism_classification
Cysteine protease
Proteolysis
Collagenase
biology.protein
Cattle
Collagen
Serine Proteases
Carica
Sequence Alignment
Biotechnology
medicine.drug
Subjects
Details
- ISSN :
- 13476947
- Volume :
- 85
- Database :
- OpenAIRE
- Journal :
- Bioscience, Biotechnology, and Biochemistry
- Accession number :
- edsair.doi.dedup.....b499897227b590bc580629ed9b156797
- Full Text :
- https://doi.org/10.1093/bbb/zbab025