Primary structure of Dioclea glabra trypsin inhibitor, DgTI, a Bowman-Birk inhibitor

Primary structure of Dioclea glabra trypsin inhibitor, DgTI, a Bowman-Birk inhibitor

Autor Bueno, N. R. Google Scholar
Fritz, H. Google Scholar
Auerswald, E. A. Google Scholar
Mentele, R. Google Scholar
Sampaio, M. Google Scholar
Sampaio, CAM Google Scholar
Oliva, MLV Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Univ Munich
Resumo 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.
Assunto Dioclea glabra
Bowman-Birk inhibitor
trypsin inhibitor
amino acid sequence
Idioma Inglês
Data 1999-08-11
Publicado em Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc, v. 261, n. 3, p. 838-843, 1999.
ISSN 0006-291X (Sherpa/Romeo, fator de impacto)
Editor Academic Press Inc
Extensão 838-843
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000082014900050

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