Partial purification of plasma phenoloxidase of the yellow fever mosquito Aedes aegypti L. (Diptera: Culicidae)

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 chromatog...

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Bibliographic Details
Published in:Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology 1995-03, Vol.110 (3), p.641-647
Main Authors: Burks, Charles S., Fuchs, Morton S.
Format: Article
Language:English
Subjects:
Aedes - enzymology
Aedes aegypti
Animals
Chromatography, Gel
Chromatography, Ion Exchange
Culicidae
Detection method
Diptera
Freshwater
Molecular Weight
Monophenol Monooxygenase - chemistry
Monophenol Monooxygenase - isolation & purification
Mosquito
Plasma phenoloxidase
Protein Conformation
Protein purification
Tyrosinase
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Summary: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.
ISSN:1096-4959
0305-0491
1879-1107
DOI:10.1016/0305-0491(94)00166-R