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

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

Author Pando, S. C. Google Scholar
Oliva, MLV Google Scholar
Sampaio, CAM Google Scholar
Di Ciero, L. Google Scholar
Novello, J. C. Google Scholar
Marangoni, S. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Universidade Estadual de Campinas (UNICAMP)
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. (C) 2001 Elsevier B.V. All rights reserved.
Keywords Delonix regia
Kunitz inhibitor
serine proteinase
human plasma kallikrein
Language English
Date 2001-07-01
Published in Phytochemistry. Oxford: Pergamon-Elsevier B.V., v. 57, n. 5, p. 625-631, 2001.
ISSN 0031-9422 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 625-631
Access rights Closed access
Type Article
Web of Science ID WOS:000169481100002

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