Purification of a DNA-binding protein from Xenopus laevis unfertilized eggs.
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.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D004257:DNA Polymerase II / Q000378:metabolism; D004789:Enzyme Activation; D005260:Female; D007700:Kinetics; D008970:Molecular Weight; D010063:Ovum / Q000378:metabolism; D014981:Xenopus
D000596:Amino Acids; D002352:Carrier Proteins; D004247:DNA; D004257:DNA Polymerase II