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Purification and Characterization of a Collagenase from the Mackerel, Scomber japonicus
( Pyo Jam Park ),( Sang Hoon Lee ),( Hee Guk Byun ),( Seo Hyun Kim ),( Se Kwon Kim ) 생화학분자생물학회 2002 BMB Reports Vol.35 No.6
Collagenase from the internal organs of a mackerel was purified using acetone precipitation, ion-exchange chromatography on a DEAE-Sephadex A-50, gel filtration chromatography on a Sephadex G-100, ion-exchange chromatography on DEAE-Sephacel, and gel filtration chromatography on a Sephadex G-75 column. The molecular mass of the purified enzyme was estimated to be 14.8 kDa by gel filtration and SDS-PAGE. The purification and yield were 39.5-fold and 0.1% when compared to those in the starting-crude extract. The optimum pH and temperature for the enzyme activity were around pH 7.5 and 55℃, respectively. The K_m and V_max of the enzyme for collagen Type I were approximately 1.1 mM and 2,343 U, respectively. The purified enzyme was strongly inhibited by Hg^2+, Zn^2+, PMSF, TLCK, and the soybean-trypsin inhibitor.