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

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Data
1992-01-01
Autores
Oliva, Maria Luiza Vilela [UNIFESP]
Mendes, Catarina Ruas [UNIFESP]
Bueno, Norlene Regina [UNIFESP]
Honda, N. K.
Sampaio, Misako Uemura [UNIFESP]
Sampaio, Claudio Augusto Machado [UNIFESP]
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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.
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Brazilian Journal Of Medical And Biological Research. Sao Paulo: Assoc Bras Divulg Cientifica, v. 25, n. 10, p. 999-1002, 1992.
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