Format

Send to

Choose Destination
Phytochemistry. 2001 Jul;57(5):625-31.

Primary sequence determination of a Kunitz inhibitor isolated from Delonix regia seeds.

Author information

1
Department of Biochemistry, Institute of Biology, UNICAMP, 13083-970, Campinas-SP, Brazil

Abstract

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.

PMID:
11397427
DOI:
10.1016/s0031-9422(01)00080-2
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center