Abstract
A fibrinolytic enzyme has been isolated from the edible honey mushroom, Armillariella mellea and purified. The apparent molecular mass of purified enzyme was estimated to be 19800Da by SDS polyacryl amide gel electrophoresis and 19900Da by gel filtration, indicating that it was a monomer. The enzyme was optimal at pH 7, suggesting that the purified enzyme was a neutral proteinase. It shows the maximum fibrinolytic activity at $55^{\circ}C$, is completely inactivated above $65^{\circ}C$, and still indicates 40% of activity at $37^{\circ}C$. The fibrinolytic activity has been decreased by the addition of EDTA. Fifteen amino acid sequence was determined by protein sequencing techniques.
뽕나무버섯 추출물에서 fibrinolytic enzyme을 분리 정제하였다. 이 효소의 분자량은 약 19800Da 이고 pH 7.0에서 최고의 활성을 보여주는 neutral protease로 $55^{\circ}C$에서 최대 활성을 나타냈다. EDTA에 의해 활성이 저해되는 것으로 보아 metalloprotease로 추정되며 $Hg^{+2}$의 영향을 받아 활성이 상실되었다. N-terminal amino acid 분석 결과 15번째까지의 아미노산 잔기 순서는 X-X-T-N-G-X-T-X-S-R-Q-T-T-L-V 이었으며 지금까지 알려진 것과는 다른 새로운 효소이다.
