PMID: 6539127Jun 16, 1984Paper

Structural and functional heterogeneity of single-stranded DNA-binding proteins from calf thymus

Biochimica Et Biophysica Acta
O ValentiniS Riva

Abstract

A new purification technique for 'single-stranded DNA-binding proteins' from calf thymus permits the demonstration of a considerable heterogeneity within these proteins. Several molecular species are obtained with Mr between 24.10(3) and 30.10(3) and pI values between 6 and 8, showing significant differences with regard to the following functional properties: strength of binding to single-stranded DNA; lowering of melting temperature of poly[d(A-T)]; stimulation of DNA polymerase alpha on a poly[d(A-T)] template. Analysis of trypsin digestion products demonstrates that the different molecular species share extensive primary sequence homology. Experiments with antibodies show that the different molecular species are antigenically related and that a 31 kDa protein present in low amounts in our preparations is very cross-reactive.

References

May 12, 1975·Analytical Biochemistry·W I Otavsky, J W Drysdale
Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
Feb 15, 1977·European Journal of Biochemistry·B OttoR Knippers
Jun 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·P Palese, J L Schulman
Oct 16, 1980·Biochemical and Biophysical Research Communications·S RivaF Cobianchi

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Citations

Sep 1, 1985·Proceedings of the National Academy of Sciences of the United States of America·K R WilliamsS R Planck
Feb 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·A Y Jong, J L Campbell
Feb 11, 1998·Experimental Lung Research·H H RayaniJ Floros
Feb 1, 1986·Bioscience Reports·L N MarekovB G Beltchev
Jul 31, 1992·Biochimica Et Biophysica Acta·R RajpurohitS Kim

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