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Title 

Purification and characterization of Thermus caldophilus GK24 DNA polymerase

Authors 

Jong Hoon ParkJoon Su KimSuk Tae KwonDae Sil Lee

Publisher 

Federation of European Biochemical Societies

Issue Date 

1993

Citation 

European Journal of Biochemistry, vol. 214, no. 0, pp. 135-140

Keywords 

dna polymeraseenzyme purificationthermusDNA-directed DNA polymerasepolymerase chain reaction

Abstract 

A thermostable DNA polymerase from Thermus caldophilus GK24 was purified to near homogeneity by chromatographic methods, including ion-exchange, gel-filtration and affinity chromatography. The purified enzyme had a specific activity of 8400 U/mg at 75°C and a lecular mass of 95 kDa, estimated by SDS/PAGE and Superose-12 gel filtration. Reaction conditions were investigated in terms of pH, metal-ion concentration and temperature. Experimental results showed that T. caldophilus (Tca) DNA polymerase had a maximum activity near pH 8.7 at 75 °C. The N-terminal sequence of the enzyme was highly similar to that of Thermus aquaticus (Taq) DNA polymerase, which was consistent with the fact that the enzyme had 5'-to-3' exonuclease activity and no 3'-to-5' exonuclease activity. Gene amplification using Tca DNA polymerase resulted in longer products than amplification using Taq DNA polymerase.

ISSN 

0014-2956

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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