말똥 성게를 인공 수정시킨 후 column chromatography 법으로 DNA polymerase α를 분리 정제하였다. Sephadex G-200과 SDS polyacryamide gel electophoresis에 의한 DNA polymerase α의 분자량은 약 137,000∼138,000이였다. 효소활성의 최적 pH는 7.4였고, 칼슘이온 20mM, 나트륨이온 25mM에서 활성이 높았고, 마그네슘 이온은 10mM일 때 활성이 높았다. DNA polymerase α는 N-ethylmaleimide, aphidicolin, cytosin β-D-arabinofuranoside 5′-triphosphate (ara CTP)와 phosphonoacetic acid에 의하여 활성이 크게 저하되었다.

From the sea-urchin, Hemicentrotus pulcherrismus, we have purified by four column chromatographic steps for DNA polymerase α activity. The molecular weight of DNA polymerase α was determined to be around 137,000-138,000 by Sephadex G-200 gel filtration and SDS-polyacrylamide gel electrophoresis. The purified enzyme had the optimal activity at pH 7.4. This enzyme showed to be a function of the metal ion K^+, Na^+ and Mg^(2+) employed as activators, the optimum K^+ or Na^+ concentration were 20mM or 25mM and the optimum Mg^(2+) concentration was 10mM. The enzyme activity was inhibited by N-ethyl-maleimide, aphidicolin, cytosine β-D-arabinofuranoside 5′-triphoshate (ara CTP) and phosphonoacetic acid.