PURIFICATION and PARTIAL CHARACTERIZATION of A SCHIZOLOBIUM-PARAHYBA CHYMOTRYPSIN INHIBITOR

PURIFICATION and PARTIAL CHARACTERIZATION of A SCHIZOLOBIUM-PARAHYBA CHYMOTRYPSIN INHIBITOR

Autor Souza, EMT Google Scholar
Mizuta, K. Google Scholar
Sampaio, M. U. Google Scholar
Sampaio, CAM Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Universidade de Brasília (UnB)
LMU
Resumo Schizolobium parahyba seed chymotrypsin inhibitor (SPC) is a protein with M(r) of 20 000 and four half-cystine residues and no free thiol group. SPC is stable at temperatures up to 75 degrees at pH 7 but gradually loses activity when kept at 95 degrees for 1 hr and total inactivation occurs after 5 hr. Amino acid analysis shows a high content of glycine, aspartate, glutamate and alanine residues. A pi of 4.52 predicted from the amino acid content agrees with experimental results. A stable binary complex with M(r) of 45 000, Ki = 5.85 x 10(-8) M and molar ratio of 1:1 is formed between SPC and chymotrypsin. the determined single N-terminal sequence of SPC shows homology with Kunitz type soybean trypsin inhibitors.
Palavra-chave SCHIZOLOBIUM PARAHYBA
LEGUMINOSAE
PROTEINASE INHIBITOR
CHYMOTRYPSIN, KUNITZ INHIBITOR
PROTEINASE
Idioma Inglês
Data de publicação 1995-06-01
Publicado em Phytochemistry. Oxford: Pergamon-Elsevier B.V., v. 39, n. 3, p. 521-525, 1995.
ISSN 0031-9422 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 521-525
Fonte http://dx.doi.org/10.1016/0031-9422(94)00921-F
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:A1995RH33200008
Endereço permanente http://repositorio.unifesp.br/handle/11600/25501

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