Effect of alpha-1-antichymotrypsin on activity of DNA primase isolated from human stomach adenocarcinoma cells.
This paper describes an investigation into the effect of alpha-1-antichymotrypsin (ACT) on DNA primase. DNA primase was partially purified from human stomach carcinoma cells. It was found that poly(dC)-dependent DNa primase activity was inhibited by ACT and the inhibition was proportional to the concentration of the inhibitor. The inhibitory effect of ACT remained even after ACT lost most of its chymotrypsin-inhibitory activity by heat treatment. Poly(dT)-dependent primase activity was enhanced by the presence of ACT. The enhancement was effective up to a concentration of 1mg/ml.
Takada
S
S
Department of Biochemistry, School of Medicine, Tokai University, Kanagawa, Japan.
Tsuda
M
M
Yamamura
M
M
Katsunuma
T
T
D000230:Adenocarcinoma / Q000201:enzymology*; D019915:DNA Primase; D004795:Enzyme Stability; D006801:Humans; D007700:Kinetics; D012316:RNA Nucleotidyltransferases / Q000302:isolation & purification / Q000378:metabolism*; D013274:Stomach Neoplasms / Q000201:enzymology*; D000514:alpha 1-Antichymotrypsin / Q000494:pharmacology*
D000514:alpha 1-Antichymotrypsin; D019915:DNA Primase; D012316:RNA Nucleotidyltransferases