Autor(es): Burks C S; Fuchs M S

Resumo: A nitrocellulose-based assay was developed using a dot-blot apparatus to detect phenoloxidase activity in column fractions. Using this assay, plasma phenoloxidase was partially purified from Aedes aegypti larvae using hydrophobic interaction chromatography, gel filtration, and ion-exchange chromatography. The molecular weight (M(r)) native enzyme was 130,000, and it contained subunits of 76,000, 62,000, and 58,000. Two phenoloxidase peaks were observed by ion exchange chromatography, and these fractions had distinct polypeptide profiles as detected by SDS-PAGE.

Palavras-Chave: Aedes aegypti; Mosquito; Plasma phenoloxidase; Tyrosinase; Detection method; Protein purification

Imprenta: Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, v. 110, n. 3, p. 641-647, 1995

Identificador do objeto digital: 10.1016/0305-0491(94)00166-R

Descritores: Aedes aegypti - Molecular Structure

Data de publicação: 1995

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