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Title: Primary structure of Dioclea glabra trypsin inhibitor, DgTI, a Bowman-Birk inhibitor
Authors: Bueno, N. R.
Fritz, H.
Auerswald, E. A.
Mentele, R.
Sampaio, M.
Sampaio, CAM
Oliva, MLV
Universidade Federal de São Paulo (UNIFESP)
Univ Munich
Keywords: Dioclea glabra
Bowman-Birk inhibitor
trypsin inhibitor
amino acid sequence
Issue Date: 11-Aug-1999
Publisher: Academic Press Inc
Citation: Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc, v. 261, n. 3, p. 838-843, 1999.
Abstract: A novel serine proteinase inhibitor, DgTI, was purified from Dioclea glabra seeds by acetone precipitation, and ion-exchange and reverse phase chromatography. the inhibitor belongs to the Bowman-Birk family, and its primary sequence, determined by Edman degradation and mass spectrometry, of 67 amino acids is: SSGPCCDRCRCTKSEPPQCQCQDVRLNSC-HSACEACVCSHSMPGLCSCLDITHFCHEPCKSSGD- DED, Although two reactive sites were determined by susceptibility to trypsin (Lys(13) and His(40)), the inhibitory function was assigned only to the first site. the inhibitor forms a 1:1 complex with trypsin, and Ki is 0.5 x 10(-9) M. Elastase, chymotrypsin, kallikreins, factor Xa, thrombin, and plasmin were not inhibited. By its properties, DgTI is a Bowman-Birk inhibitor with structural and inhibitory properties between the class of Bowman-Birk type I (with a fully active second reactive site), and Bowman-Birk type II (devoid of second reactive site). (C) 1999 Academic Press.
ISSN: 0006-291X
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