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Amino Acid Sequences of Double-headed Proteinase Inhibitors from the Seeds ofCanavalia lineata
- Source :
- Bioscience, Biotechnology, and Biochemistry. 58:376-379
- Publication Year :
- 1994
- Publisher :
- Informa UK Limited, 1994.
-
Abstract
- The amino acids of two Bowman-Birk type proteinase inhibitors (CLTI-I and -II) from the seeds of Canavalia lineata were sequenced by a manual Edman degradation using the DABITC/PITC double coupling method after enzymatic digestions with Achromobacter lyticus lysyl endopeptidase, Staphylococcus aureus V8 protease, and chymotrypsin. CLTI-I contains 75 amino acid residues. CLTI-II has an identical sequence to CLTI-I except an extra Asp residue attached at the C-terminus. The inhibitors showed a homology (40-70%) to other Bowman-Birk inhibitors. The reactive-site peptide bonds were estimated to be Lys21-Ser22 and Leu48-Ser49 against trypsin and chymotrypsin, respectively. An inhibitory active fragment containing only the chymotrypsin-reactive site was also described.
- Subjects :
- medicine.medical_treatment
Molecular Sequence Data
Applied Microbiology and Biotechnology
Biochemistry
Analytical Chemistry
Lysyl endopeptidase
medicine
Peptide bond
Protease Inhibitors
Amino Acid Sequence
Disulfides
Molecular Biology
chemistry.chemical_classification
Binding Sites
Protease
Chymotrypsin
Sequence Homology, Amino Acid
biology
Edman degradation
Hydrolysis
Organic Chemistry
General Medicine
Plants
Canavalia
biology.organism_classification
Trypsin
Peptide Fragments
Amino acid
chemistry
Seeds
biology.protein
Biotechnology
medicine.drug
Subjects
Details
- ISSN :
- 13476947 and 09168451
- Volume :
- 58
- Database :
- OpenAIRE
- Journal :
- Bioscience, Biotechnology, and Biochemistry
- Accession number :
- edsair.doi.dedup.....5132659afc982a46b88d6b9d228cdd23