These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Malate dehydrogenase of a mosquito, Culex p. quinquefasciatus: developmental changes, polymorphism, and physicochemical characterization.
    Author: Narang S, Narang N.
    Journal: Biochem Genet; 1975 Feb; 13(1-2):73-84. PubMed ID: 1137567.
    Abstract:
    Malate dehydrogenase (MDH) of larval, pupal, and adult stages of Culex p. quinquefasciatus has been characterized by electrophoresis, isoelectric focusing, and other physicochemical means. It exists as a multiple molecular form possessing a large number of isoenzymes, from a minimum of three in early instar larvae to as many as 14 in adults. The isoenzyme pattern changes during development with respect to both relative activity and the appearance of some new forms and disappearance of others. Each developmental stage possesses a characteristic electrophoretic and gel isoelectric focusing pattern. MDH isoenzymes differ in their response to heat and thiol reagents. Similar electrophoretic variants from larvae, pupae, and adults show great differences in their response to heat treatment at 50 C and 56 C, indicating some differentiation of isoenzymes in each stage of development. Homogenization of whole mosquitos in mercaptoethanol solution results in a sharp increase in the activity of the principal bands and a decrease or disappearance of minor ones. The possibility of some minor bands being "conformers" arising due to nongenetic factors is discussed.
    [Abstract] [Full Text] [Related] [New Search]