Autor(es): Gollas-Galvan, T; Hernandez-Lopez, J; Vargas-Albores, F

Resumo: Prophenoloxidase (proPO) was purified from blood cells of the brown shrimp Penaeus californiensis by ultracentrifugation and dye affinity chromatography. The isolated proPO is a 114-kDa monomeric protein as determined by SDS-PAGE. This protein can be hydrolyzed by proteinases, producing a 107-kDa active phenoloxidase (PO). The isoelectric point for both protein forms was 7.35. The PO reaction using L-DOPA as substrate, has an optimum pH of 8, and was poorly inhibited by sodium azide, thiourea and EDTA, but strongly inhibited by diethyl thiocarbamate. According to the substrate affinity and inhibition characteristics, this phenoloxidase was classified as a tyrosinase-like phenoloxidase. Purified proPO was not activated by bacterial lipopolysaccharides or beta-glucans. (C) 1999 Elsevier Science Inc. All rights reserved.

Palavras-Chave: proPO; Defense system; Invertebrate immunology; Shrimp immunity; PPAE; o-diphenoloxidase; Tyrosinase; L-DOPA; Blue sepharose

Imprenta: Comparative Biochemistry and Physiology B-Biochemistry & Molecular Biology, v. 122, n. 1, p. 77-82, 1999

Identificador do objeto digital: 10.1016/S0305-0491(98)10143-8

Descritores: Aedes aegypti - Immunology

Data de publicação: 1999

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