EFFECT OF ALPHA-1-ANTICHYMOTRYPSIN ON ACTIVITY OF DNA PRIMASE ISOLATED FROM HUMAN STOMACH ADENOCARCINOMA CELLS
- 1 May 1988
- journal article
- research article
- Vol. 16 (5) , 949-954
Abstract
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 1 mg/ml.This publication has 15 references indexed in Scilit:
- Novel form of DNA polymerase alpha associated with DNA primase activity of vertebrates. Detection with mouse stimulating factor.Journal of Biological Chemistry, 1983
- The Biological Activity of α-1-Antichymotrypsin: The Change of Chymotrypsin-Inhibitory and Immunoenhancing Activities by Heat Treatment1The Journal of Biochemistry, 1982
- HUMAN ALPHA-1-ANTICHYMOTRYPSIN ENHANCES PRIMARY ANTIBODY-RESPONSE IN THE MOUSE1982
- ANALYSIS OF THE TISSUE AND CELLULAR-LOCALIZATION OF ALPHA-1-ANTICHYMOTRYPSIN BY AN IMMUNOHISTOCHEMICAL TECHNIQUE1982
- Enhancement by α-1-antichymotrypsin of antibody response in vivoBiochemical and Biophysical Research Communications, 1981
- Purification of a serum DNA binding protein (64DP) with a molecular weight of 64,000 and its diagnostic significance in malignant diseasesBiochemical and Biophysical Research Communications, 1980
- The degradation of human lung elastin by neutrophil proteinasesBiochimica et Biophysica Acta (BBA) - Protein Structure, 1979
- Human α-1-antichymotrypsin: interaction with chymotrypsin-like proteinasesBiochemistry, 1978
- Human α-1-antichymotrypsin: purification and propertiesBiochemistry, 1978
- DISC ELECTROPHORESIS – II METHOD AND APPLICATION TO HUMAN SERUM PROTEINS*Annals of the New York Academy of Sciences, 1964