Primary sequence determination of a Kunitz inhibitor isolated from Delonix regia seeds
| Autor: | Sergio Marangoni, José C. Novello, Luciana Di Ciero, Claudio A. M. Sampaio, Maria Luiza Vilela Oliva, Silvana Cristina Pando |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Molecular Sequence Data
Plant Science Horticulture Biology Biochemistry Serine medicine Amino Acid Sequence Molecular Biology Peptide sequence Chromatography High Pressure Liquid Plant Proteins chemistry.chemical_classification Plants Medicinal Sequence Homology Amino Acid Kunitz STI protease inhibitor Edman degradation Fabaceae General Medicine Chromatography Ion Exchange Trypsin biology.organism_classification Molecular biology Amino acid chemistry Enzyme inhibitor Seeds Chromatography Gel biology.protein Electrophoresis Polyacrylamide Gel Peptides Trypsin Inhibitors Delonix regia medicine.drug |
| Zdroj: | Phytochemistry. 57:625-631 |
| ISSN: | 0031-9422 |
| DOI: | 10.1016/s0031-9422(01)00080-2 |
| Popis: | A serine proteinase inhibitor was purified from Delonix regia seeds a Leguminosae tree of the Caesalpinioideae subfamily. The inhibitor named DrTI, inactivated trypsin and human plasma kallikrein with K(i )values 2.19x10(-8) M and 5.25 nM, respectively. Its analysis by SDS-PAGE 10-20% showed that the inhibitor is a protein with a single polypeptide chain of M(r) 22 h Da. The primary sequence of the inhibitor was determined by Edman degradation, thus indicating that it contained 185 amino acids and showed that it belongs to the Kunitz type family; however, its reactive site did not contain Arg or Lys at the putative reactive site (position 63, SbTI numbering) or it was displaced when compared to other Kunitz-type inhibitors. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect