SEPARATION OF THE PROTEIN CONSTITUENTS OF THE LARVAL DIETS OF THE HONEYBEE BY CONTINUOUS PAPER ELECTROPHORESIS

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Abstract
The protein constituents of the larval diets of queen and worker honeybees were separated by continuous paper electrophoresis. The electrophoretic patterns of royal jelly of any age and the early worker diet were similar and comprised five ninhydrin-reactive bands or fractions. Fraction 1 (nearest the cathode) contained lysine as a free amino acid. Fractions 3 and 4 appeared to be complex polypeptides. Alanine, asparagine, aspartic acid, glutamic acid, glycine, histidine, isoleucine and/or leucine, lysine, phenylalanine, threonine, tyrosine, valine, and an unidentified substance were found in chromatograms of the acid hydrolyzate of fraction 3; the hydrolyzate of fraction 4 contained the same amino acids except for threonine. Fractions 2 and 5 were not characterized. Electrophoresis of the diet of worker larvae older than 3 days showed a pronounced fading of all bands, attributable to the dilution of the solids by the addition of honey which occurs at this time. There appeared to be no qualitative differences between the protein fractions of royal jelly and worker diet which would account for the differentiation of female honeybees into queens and workers. The decrease with age in the percentage of protein in the worker diet may be significant.

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