-transparent.png){kind=logo}
An enzyme, which is probably identical with polynucleotide phosphorylase, was prepared from Escherichiacoli B. In the presence of Mn(2+) it catalyzes the addition of one (and to a slight extent more) residue of deoxyribonucleotide residue from the diphosphate to an oligodeoxyribonucleotide primer. The shortest effective primers contained three phosphate residues. Ribodinucleotides were effective as primers and accepted two or three deoxyribonucleotide residues under these conditions. The application of the procedures to the convenient synthesis of certain defined oligodeoxyribonucleotides up to nine residues long is discussed.
Related Publications
S Gillam, and
K Waterman, and
M Doel, and
M Smith
August 1972,
Nature: New biology,
S Gillam, and
K Waterman, and
M Doel, and
M Smith
December 1974,
Nucleic acids research,
S Gillam, and
K Waterman, and
M Doel, and
M Smith
April 1963,
Biochemical and biophysical research communications,
S Gillam, and
K Waterman, and
M Doel, and
M Smith
May 1988,
FEBS letters,
S Gillam, and
K Waterman, and
M Doel, and
M Smith
April 1978,
The Journal of biological chemistry,
S Gillam, and
K Waterman, and
M Doel, and
M Smith
October 1987,
DNA (Mary Ann Liebert, Inc.),
S Gillam, and
K Waterman, and
M Doel, and
M Smith
January 1977,
Proceedings of the National Academy of Sciences of the United States of America,
S Gillam, and
K Waterman, and
M Doel, and
M Smith
April 1965,
Science (New York, N.Y.),
S Gillam, and
K Waterman, and
M Doel, and
M Smith
January 1963,
Experientia,
S Gillam, and
K Waterman, and
M Doel, and
M Smith
July 1976,
Journal of biochemistry,
