Autor(es): Jarrouge, M. G.; Capurro, M. L.; Bianchi, A. G.; Marinotti, O.

Resumo: Aedes aegypti larval hemolymph proteins were analyzed, and the major protein was characterized. The major protein, designated P1, is hexameric and is composed of subunits with molecular weights estimated to be 83,000. P1 is dissociated into its subunits when the pH is elevated from 7 to 9. This protein accumulates during the last larval instar and is not detected in adult mosquitoes. These characteristics, together with the high content of aromatic amino acids, include P1 in the arylphorin group of the insect storage proteins.

Palavras-Chave: Molecular structure; Insect larvae; Proteins; Hemolymph; Protein structure; Aedes aegypti; Culicidae

Imprenta: Archives of Insect Biochemistry and Physiology, v. 34, n. 2, p. 191-201, 1997.

Descritores: Aedes aegypti - Molecular Structure ; Aedes aegypti - Proteins

Data de publicação: 1997