CYSTEINE PROTEINASE-INHIBITORS IN LICHEN (COLLEMA-LEPTOSPORUM MALME)

CYSTEINE PROTEINASE-INHIBITORS IN LICHEN (COLLEMA-LEPTOSPORUM MALME)

Author Oliva, Maria Luiza Vilela Autor UNIFESP Google Scholar
Mendes, Catarina Ruas Autor UNIFESP Google Scholar
Bueno, Norlene Regina Autor UNIFESP Google Scholar
Honda, N. K. Google Scholar
Sampaio, Misako Uemura Autor UNIFESP Google Scholar
Sampaio, Claudio Augusto Machado Autor UNIFESP Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
UNIV FED MATO GROSSO SUL
Abstract Aqueous extracts of the lichen Collema leptosporum contain a cysteine proteinase inhibitor (0.48 mg equivalent/g acetone powder) and a serine proteinase inhibitor (1.28 mg equivalent/g acetone powder) and a peptidase that hydrolyzes Ac-Phe-Arg-Nan. Ion-exchange chromatography using SP-Sephadex and DEAE-Sephadex followed by gel filtration purified three forms of inhibitor. The papain inhibition fits Morrison's slow tight binding model and the dissociation constants (Ki) were 280,8.2 and 0.63 nM for inhibitors I, II and III, respectively. The molecular weight of the three inhibitors, estimated by filtration using Superose 12 and SDS-PAGE was approximately 20,000.
Keywords CYSTEINE PROTEINASES
ENZYME INHIBITORS
LICHENS
PROTEOLYSIS
Language English
Date 1992-01-01
Published in Brazilian Journal Of Medical And Biological Research. Sao Paulo: Assoc Bras Divulg Cientifica, v. 25, n. 10, p. 999-1002, 1992.
ISSN 0100-879X (Sherpa/Romeo, impact factor)
Publisher Assoc Bras Divulg Cientifica
Extent 999-1002
Access rights Closed access
Type Article
Web of Science ID WOS:A1992JX83100005
URI http://repositorio.unifesp.br/11600/43013

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