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Major hemolymph protein of Aedes aegypti larvae
Author(s) -
Jarrouge Marcio Georges,
de Lara Capurro Margareth,
de Bianchi Antonio Gildo,
Marinotti Osvaldo
Publication year - 1997
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/(sici)1520-6327(1997)34:2<191::aid-arch5>3.0.co;2-#
Subject(s) - hemolymph , aedes aegypti , biology , larva , instar , insect , biochemistry , amino acid , botany
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. Arch. Insect Biochem. Physiol. 34:191–201, 1997. © 1997 Wiley‐Liss, Inc.