http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : 황영선ㆍ김강화 (검색결과 4 건)
- 무료
- 기관 내 무료
- 유료
-
Haemophilus influenzae 티올 과산화효소의 특성
황영선ㆍ김강화 전남대학교 가정과학연구소 2000 生活科學硏究 Vol.10 No.-
Haemophilus influenzae HI0571 protein that shows homology to E. coli thiol peroxidase uses yeast thioredoxin system as an electron donor[Hwang. Y. S., Chae. H. Z. and Kim. K. (2000) J. Biochem. Mol. Biol. 33, 514∼518]. The microorganism has two open reading frames, HI1158 and HI0084, showing homology to a thioredoxin reductase and a thioredoxin, respectively. Both proteins consisting thioredoxin system were expressed in E. coli, and then the proteins were subsequently purified. The H. influenzae thioredoxin system showed 5,5'-dithiobis- (2-nitrobenzoic acid) reduction activity. H. influenzae HI0751 protein, thiol peroxidase was characterized using the thioredoxin system as an electron donor. The thiol peroxidase showed the thioredoxin dependent peroxidase activity. And glutamine synthetase protection activity of thiol peroxidase against Thiol/Fe3+/O2 system was enhanced by addition of the thioredoxin. An antioxidant function of thiol peroxidase in intact cells was demonstrated by the observation that E. coli cells overexpressed with H. influenzae thiol peroxidase were less sensitive to growth inhibition by alkyl hydroperoxides.
-
Haemophilus influenzae 티올 과산화효소의 특성
황영선(Young Sun Hwang),김강화(Kanghwa Kim) 전남대학교 생활과학연구소 2000 生活科學硏究 Vol.10 No.-
Haemophilus influenzae HI0571 protein that shows homology to E. coli thiol peroxidase uses yeast thioredoxin system as an electron donor[Hwang. Y. S., Chae. H. Z., and Kim. K. (2000) J. Biochem. Mol. Biol. 33, 514~518]. The microorganism has two open, reading frames. HI1158 and HI0084, showing homology to a thioredoxin reductase and a thioredoxin, respectively. Both proteins consisting thioredoxin system were expressed in E. coli, and then the proteins were subsequently purified. The H. influenzae thioredoxin system showed 5.5’-dithiobis-(2-nitrobenzoic acid) reduction activity. H, influenzae HI0751 protein, thiol peroxidase was characterized using the thioredoxin system as an electron donor. The thiol peroxidase showed the thioredoxin dependent peroxidase activity. And glutamine synthetase protection activity of thiol peroxidase against Thiol/Fe<sup>3+</sup>/O₂ system was enhanced by addition of the thioredoxin. An antioxidant function of thiol peroxidase in intact cells was demonstrated by the observation that E. coli cells overexpressed with H. influenzae thiol peroxidase were less sensitive to growth inhibition by alkyl hydroperoxides.
-
기해진,황영선,김강화,홍윤호 한국축산식품학회 1998 한국축산식품학회지 Vol.18 No.1
In order to study the tenderizing effect of the proteolytic enzyme, ficin, from fig fruit (Ficus carica L), the enzyme was purified from fig latex by precipitation and chromatography. The ficin separated from Bongraesi showed single band on SDS-PAGE. However, the ficin from Masui showed tow bands. The specific activity of ficin purified from Bongraesi species was 2.8 unit/mg protein and that from Masui species was 6.5 unit / mg protein. The amounts of ficin purified from 50 mL of crude latex of Bongraesi and Masui were 1,760 mg and 657 mg, respectively. the water holding capacity of beef decreased to the large extent, when sugar Bongraesi latex and Masui latex were added. The hardness of beef showed decreasing tendency with the time, however, after 60 min, it decreased and thereafter increased a little after 120 min. the hardness of beef decreased sharply with addition of the latex of Bongraesi and Masui. The Masui has more tenderizing effect than the Bongraesi. When meat was mixed with tenderizing agent(ficin) and not heated, the change of color showed significant difference (p<0.01). when meat was mixed with tenderizing agent(ficin) and heated, the toughness showed significant difference (p<0.01) and the softness showed significant difference (p<0.001).
-
연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
