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Purification and properties of mosquito DNA polymerase.
J Biol Chem ; 253(6): 1978-83, 1978 Mar 25.
Article em En | MEDLINE | ID: mdl-24632
For the first time, DNA polymerase in a postembryonic insect has been purified and characterized. This enzyme from mosquito larvae was purified 1700-fold and was free of deoxyribonuclease and protease activities, which hindered previous investigations of insect polymerases. The enzyme had a molecular weight of 132,000 by gen filtration and aggregated to higher molecular weights when concentrated. With an activated DNA template, the pH optimum was 7.2 in phosphate buffer, and the Mg2+ concentration optimum was 5 to 10 mM. Polymerase activity was inhibited by the antisulfhydryl reagents, N-ethylmaleimide and p-mercuribenzoate, and by KCl. These properties indicate that the mosquito enzyme resembles mammalian alpha-polymerase but differs in its lack of inhibition to low ethanol concentrations. There was no evidence of a beta-polymerase form in the mosquito.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: DNA Polimerase Dirigida por DNA / Culicidae Limite: Animals Idioma: En Ano de publicação: 1978 Tipo de documento: Article
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: DNA Polimerase Dirigida por DNA / Culicidae Limite: Animals Idioma: En Ano de publicação: 1978 Tipo de documento: Article