Abstract
A low molecular weight DNA polymerase from ovaries of the frog Xenopus laevis. DNA polymerase-beta (ovarian).
Highlights
A low molecular weight DNA polymerase (DNA nucleotidyltransferase; EC 2.7.7.7) has been purified 265,000-fold from ovaries of the frogXertopus Zuevis
The purification and some properties of the low molecular weight DNA polymerase are described in this paper
DNA Polymeruse-P (Ovarian) of Xenopus laevis or MgCl, (0) was varied; incubation was for 30 min at 26” with 1 unit of DNA polymerase activity (Fraction VIII)
Summary
Laboratory for Biology, The Johns Hopkins (Received for publication, University, Baltimore, July 19, 1977). Most of the properties of the low molecular weight DNA polymerase purified from ovaries of X. laeuis are consistent with the enzyme being a polymerase of the /I type. DNA polymerases of the p type were defined as low molecular weight enzymes which function optimally at high pH in the presence of high concentrations of KC1 or NaCl and are resistant to sulfhydryl reagents. (9) have described two low molecular weight DNA polymerases present at similar levels in the chick embryo with molecular weights of 27,000 and 50,000. (i.e. DNA polymerase X-II ( called o( (ovarian)’ of Benbow et al [12]); and one was of low molecular weight which efficiently used poly(A) . The purification and some properties of the low molecular weight DNA polymerase are described in this paper
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