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DNA polymerase has been purified about 25,000-fold from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. On SDS-PAGE the enzyme was observed to have a molecular weight of 100 kDa and to be about 90% pure. The native molecular weight was 108 kDa indicating that the enzyme is composed of a single polypeptide. Activity gel analysis showed an active polypeptide of about 100 kDa. Under conditions promoting proteolysis this polypeptide was degraded to a slightly smaller form of 98 kDa. The enzyme has been characterized in respect to optimal assay conditions, template specificity, sensitivity to inhibitors and associated nuclease activities. The high temperature optimum of 65 degrees C should be emphasized. No substantial similarities have been found with other prokaryotic and eukaryotic DNA polymerases, although the enzyme bears certain resemblances to prokaryotic non-replicative polymerases.
L J Klimczak, and
F Grummt, and
K J Burger
January 1989,
European journal of biochemistry,
L J Klimczak, and
F Grummt, and
K J Burger
June 1979,
European journal of biochemistry,
L J Klimczak, and
F Grummt, and
K J Burger
March 1988,
The Biochemical journal,
L J Klimczak, and
F Grummt, and
K J Burger
February 1996,
Bioscience, biotechnology, and biochemistry,
L J Klimczak, and
F Grummt, and
K J Burger
February 1996,
Bioscience, biotechnology, and biochemistry,
L J Klimczak, and
F Grummt, and
K J Burger
August 1987,
Journal of biochemistry,
L J Klimczak, and
F Grummt, and
K J Burger
October 1991,
FEBS letters,
L J Klimczak, and
F Grummt, and
K J Burger
March 1990,
Biochemical and biophysical research communications,
L J Klimczak, and
F Grummt, and
K J Burger
March 1990,
Nucleic acids research,
L J Klimczak, and
F Grummt, and
K J Burger
September 1989,
Journal of bacteriology,
