Title |
Streptomyces fradiae에서 분리한 단백질 분해효소저해물질의 특성 |
Author |
정영화 · 이병규 · 이계준 |
Address |
서울대학교 자연과학대학 미생물학과 |
Bibliography |
Korean Journal of Microbiology, 28(1),65-70, 1990 |
DOI |
|
Key Words |
Proteinase inhibitor, Streptomyces fradiae |
Abstract |
The objective of the current study is to elucidate the biological roles of proteinase inhibitor in microorganisms. As the first step, a strain of Streptomyces fradiae was selected as a producer of extracellular proteinase inhibitor. The proteinase inhibitor was purified from culture broth through ultrafiltration, gel-filtration and ion-exchange chromatography. Molecular weight of the proteinase inhibitor was estimated to be 16,800 by SDS polyacrylamide gel electrophoresis. It was found that the proteinase inhibitor inhibited only alkaline serine proteinases such as subtilisin, α-chymotrypsin and Promase E but not trypsin and other proteinases. The mode of inhibition against Pronase E with succinyl-phenylalanine-p-nitroanilide as a substrate was competitive. |
Download PDF |
Kor_280110_65-70p.pdf |