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Nucleic Acids Research, 1977, Vol. 4, No. 8 2855-2870
© 1977

Articles

Purification of a DNA-binding protein from Xenopus laevis unfertilized eggs

G. Carrara{bigcirc}, S. Gattoni{bigcirc}{bigcirc}, D. Mercanti and G. P. Tocchini-Valentini

Laboratory of Cell Biology - C.N.R., Via Romagnosi 18A, 00196 Rome, Italy

Received May 26, 1977.

A DNA-binding protein from Xenopus laevis unfertilized eggs has been purified to apparent homogeneity. It is a heat stable, lysine-rich protein and has a molecular weight corresponding to 8,200 daltons, measured by sodium dodecyl sulphate gel electrophoresis. The protein, which is active in a monomeric form, stimulates DNA polymerase {propto}, and binds to single and double stranded DNA. One egg contains about 4 x 1012 molecules (minimum estimate) of the protein; since we calculate that 4 x 108 molecules are sufficient to cover the entire genome (haploid complement), there is much more protein than is needed to cover chromosomal DNA.

{bigcirc} On leave of absence from Institute of Virology - University of Rome

{bigcirc}{bigcirc} On leave of absence from Institute of General Pathology - Catholic University of Rome


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