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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 4 (1987), S. 191-203 
    ISSN: 0739-4462
    Keywords: cyanoprotein ; high molecular weight proteins ; immunology ; migratory locust ; storage proteins ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A high-molecular-weight protein, Mr 500,000, has been isolated and characterized from the hemolymph of the migratory locust, Locusta migratoria. It is composed of six seemingly identical subunits of apparent Mr 78,000. It contains low concentrations of carbohydrate and lipid, but high percentages of aspartate and glutamate as well as high proportions of hydrophobic amino acid residues. An antiserum, developed against this purified hemolymph protein, does not react in the double-diffusion test or after immunoblotting with purified lipophorin or cyanoprotein, two other major proteins in locust hemolymph. The concentration of this larval specific protein in the hemolymph of Locusta was examined during the last larval instar and in adult males by quantitative rocket immunoelectrophoresis. Its concentration increases in the second half of the fifth instar, concommitant with an increase in total protein. The protein is detectable by immunological techniques in adults, although its concentration is very low at this stage.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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