Isolation, characterization and immunological properties of ceratitin-4, a major haemolymph protein of the mediterranean fruit fly Ceratitis capitata

• Published in: Insect biochemistry Vol. 14; no. 3; pp. 285 - 291
• Main Authors: Mintzas, A.C., Reboutsicas, D.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier B.V 1984; New York, NY Pergamon Press
• Subjects: Biochemistry. Physiology. Immunology; Biological and medical sciences; Fundamental and applied biological sciences. Psychology; Insecta; Invertebrates; Physiology. Development; Ceratitis capitata; purification; major haemolymph proteins; physical-chemical characterization; Proteins; Pest; Purification; Tephritidae; Arthropoda; Insecta; Hemolymph; Invertebrata; Diptera; Physicochemical properties
• ISSN: 0020-1790
• DOI: 10.1016/0020-1790(84)90062-3

The physicochemical behaviour of the four major haemolymph proteins of the Mediterranean fruit fly Ceratitis capitata, at different pH values, has been studied by chromatography on Sephadex G-200 columns. The results show that three of these proteins (C 1, C 2, C 3) form random aggregates in acidic pH which breakdown above pH 6.5. The fourth major haemolymph protein (C 4) is a stable homohexamer of approx. 460,000 daltons up to pH 8 and dissociates reversibly in basic pH. C 4 was purified to homogeneity and it was shown to be immunologically distinct from the other three major haemolymph proteins. Immunological and electrophoretic analysis showed that C 4 remains intact up to the second day of the adult life. After this stage C 4 like the other three major haemolymph proteins seems to be utilized rapidly from the adult flies.