복령[Poria cocos (Schw.) Wolf.]중의 carboxyl proteinase을 황산 암모늄 65% 포화용액, DEAE-cellulose 및 Sephadex G-75을 이용한 gel-filtration 방법으로 분리 정제하여 그 성질을 조사하였다. 이 버섯중에서 활성분획분 I과 II을 얻었으며, 활성분획분 II에 대하여 bovine hemoglobin을 기질로 사용하여 얻은 carboxyl proteinase의 활성도의 최적 pH는 2.0, 최적온도는 $70^{circ}C$, pH 안정성은 1.2~2.5 및 열안정성은 $25^{circ}C{sim}75^{circ}C$였다. 이 효소의 subunit는 1개였고, 18종의 아미노산으로 구성된 단백질이였으며, 겉보기 분자량은 25,500(PAGE)~23,000 (HPLC)였다. 이 효소는 carbobenzoxy-L-glutamyl-L-tyrosine (CBZ-glu-tyr.)의 glutaml-L-tyrosine간의 부위를 절단하는 특이성을 가졌었다. CBZ-glu-tyr.을 사용하여 측정한 Km 값은 0.29 mM 이였다.
The enzymic properties of carboxyl proteinase isolated from the Poria cacos (Schw.) Wolf. were investigated. Two kinds of active fraction I and II were isolated from this mushroom. The active fraction II showed carboxyl proteinase activity to bovine hemoglobin substrate, and its optimum conditions were the followings; temperature, $70^{circ}C$, pH stability, 1.2~2.5 and thermal stability, $25^{circ}C{sim}75^{circ}C$. The enzyme appeared to be one subunit, and consisted of 18 kinds of amino acids. The apparent molecular weight were 25,500 (PAGE) and 23,000(HPLC), respectively. The enzyme appeared to hydrolyze peptide bond between glutaml-L-tyrosine. The Km value of this enzyme was 0.29mM when carbobenzoxy-L-tyrosine were used as a subtrate.
