Evolution of glutathione S-transferase subunits in Culicidae and related Nematocera: Electrophoretic and immunological evidence for conserved enzyme structure and expression.
Autor(es): Grant, D. F.
Resumo: The antigenic relatedness and molecular weights of glutathione S-transferase (GST) protein subunits expressed by representative members of the Dipteran suborder Nematocera were analyzed by immunoblotting and affinity chromatography. Ten species within the genus Aedes expressed two subunits which cross-reacted with an antiserum developed against the GST-1b isozyme purified from Aedes aegypti . One of these two subunits showed no discernible molecular weight variability within the ten Aedes species. Its molecular weight (25,900 Da) was identical to the GST-1a subunit found in A. aegypti . The molecular weight of the other subunits varied among the ten species, but in all cases was larger than 25,900 Da. In ten species within the genus Anopheles (considered to be among the more primitive genera in the Culicidae), only one immunologically related GST subunit was expressed. Its molecular weight was also identical to the GST-1a subunit found in the Aedes species. Members of genera considered phylogenetically intermediate between Anopheles and Aedes had either one or two cross-reacting subunits.
Palavras-Chave: Molecular structure; Biochemical composition; Enzymes; Evolution
Imprenta: Insect Biochemistry, v. 21, n. 4, p. 435-445, 1991.
Descritores: Aedes aegypti - Molecular Structure ; Aedes aegypti - Proteins
Data de publicação: 1991
