Literature DB >> 6342619

Metal content of DNA polymerase I purified from overproducing and wild type Escherichia coli.

L J Ferrin, A S Mildvan, L A Loeb.   

Abstract

DNA polymerase I purified from both E. coli strain B, and from an overproducing E. coli stain lysogenized with a lambda pol A phage were analyzed for metal content. After gel filtration to remove loosely bound metals, DNA polymerase I from both strains contained less than or equal to 0.2 gm atoms Zn2+/mole enzyme and 0.09 to 0.7 Mg2+/mole enzyme. Substoichiometric amounts of Fe, Co, Ni (less than or equal to 0.2 gm atoms), and Mn (less than or equal to 0.1 gm atoms) were detected. Since the metal content does not correlate with enzymatic activity, we conclude that DNA polymerase I is not a metalloenzyme.

Entities:  

Mesh:

Substances:

Year:  1983        PMID: 6342619     DOI: 10.1016/0006-291x(83)91522-x

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  1 in total

1.  Divalent ions attenuate DNA synthesis by human DNA polymerase α by changing the structure of the template/primer or by perturbing the polymerase reaction.

Authors:  Yinbo Zhang; Andrey G Baranovskiy; Emin T Tahirov; Tahir H Tahirov; Youri I Pavlov
Journal:  DNA Repair (Amst)       Date:  2016-05-12
  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.