Purification and characterization of a collagenase from the mackerel, Scomber japonicus.
Purification and characterization of a collagenase from the mackerel, Scomber japonicus.
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DOI：
10.5483/bmbrep.2002.35.6.576
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发表时间：
2002-11
期刊：
影响因子：
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通讯作者：
P. Park;Sang-Hoon Lee;H. Byun;Soo-Hyun Kim;Se-Kwon Kim
中科院分区：
文献类型：
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作者：
P. Park;Sang-Hoon Lee;H. Byun;Soo-Hyun Kim;Se-Kwon Kim
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 degrees, respectively. The K(m) and V(max) of the enzyme for collagen Type I were approximately 1.1mM and 2,343 U, respectively. The purified enzyme was strongly inhibited by Hg2+, Zn2+, PMSF, TLCK, and the soybean-trypsin inhibitor.
