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Purification and characterization of two Kunitz family subtilisin inhibitors from seeds of Canavalia lineata
- Source :
- Journal of biochemistry. 115(3)
- Publication Year :
- 1994
-
Abstract
- Two subtilisin inhibitors (CLSI-II and -III) were purified from seeds of Canavalia lineata by extraction with water, ammonium sulfate precipitation, and chromatographies on DEAE-Toyopearl and hydroxyapatite. The two inhibitors have the same molecular weight of about 22,000, and quite similar amino acid compositions. They contain five half-cystine residues and tend to dimerize through an intermolecular disulfide bridge due to the presence of a single cysteine residue. CLSI-III only inhibited subtilisin-type serine proteases, while CLSI-II showed a wider inhibitory specificity. Though the two inhibitors have almost identical thermal labilities, CLSI-II is more stable as to extreme pH than CLSI-III. They are considered to be Kunitz type inhibitors on the basis of several properties.
- Subjects :
- Molecular Sequence Data
Biochemistry
Serine
parasitic diseases
Protein purification
polycyclic compounds
Amino Acid Sequence
Subtilisins
Amino Acids
Molecular Biology
Ammonium sulfate precipitation
Plant Proteins
chemistry.chemical_classification
Serine protease
Plants, Medicinal
biology
Subtilisin
Fabaceae
General Medicine
biochemical phenomena, metabolism, and nutrition
bacterial infections and mycoses
Canavalia
biology.organism_classification
Chromatography, Ion Exchange
Amino acid
Molecular Weight
chemistry
Seeds
biology.protein
Electrophoresis, Polyacrylamide Gel
Cysteine
Subjects
Details
- ISSN :
- 0021924X
- Volume :
- 115
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Journal of biochemistry
- Accession number :
- edsair.doi.dedup.....50a2f20aa3f01612b5af7ab908958501