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. 1977 Aug;4(8):2855–2870. doi: 10.1093/nar/4.8.2855

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

G Carrara, S Gattoni, D Mercanti, G P Tocchini-Valentini
PMCID: PMC342614  PMID: 909794

Abstract

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 alpha, and binds to single and double stranded DNA. One egg contains about 4 x 10(12) molecules (minimum estimate) of the protein; since we calculate that 4 x 10(8) molecules are sufficient to cover the entire genome (haploid complement), there is much more protein than is needed to cover chromosomal DNA.

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Selected References

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