Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/27176
Title: Bauhinia proteinase inhibitor-based synthetic fluorogenic substrates for enzymes isolated from insect midgut and caterpillar bristles
Authors: Andrade, S. A.
Santomauro-Vaz, E. M.
Lopes, A. R.
Chudzinski-Tavassi, A. M.
Juliano, M. A.
Terra, W. R.
Sampaio, M. U.
Sampaio, CAM
Oliva, MLV
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Inst Butantan
Keywords: factor Xa
kallikrein
Kunitz inhibitor
Lonomia obliqua
plant
quenched fluorogenic substrates
sequence
serine proteinase inhibitor
Issue Date: 1-Mar-2003
Publisher: Walter de Gruyter & Co
Citation: Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 384, n. 3, p. 489-492, 2003.
Abstract: Bauhinia ungulata factor Xa inhibitor (BuXI) inactivates factor Xa and LOPAP, a prothrombin activator proteinase isolated from the venom of Lonomia obliqua caterpillar bristles. the reactive site of the enzyme inhibitor interaction was explored to design specific substrates for both enzymes. Methionine is crucial for LOPAP and factor Xa substrate interaction, since the change of both Met residues in the substrates abolished the hydrolysis. Synthetic substrates containing the sequence around the reactive site of BbKI, a plasma kallikrein inhibitor, were shown to be specific for trypsin hydrolysis. Therefore, these substrates may be an alternative in studies aiming at a characterization of trypsinlike enzyme activities, especially nonmammalian enzymes.
URI: http://repositorio.unifesp.br/handle/11600/27176
ISSN: 1431-6730
Other Identifiers: http://dx.doi.org/10.1515/BC.2003.055
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