期刊
BIOTECHNOLOGY LETTERS
卷 25, 期 22, 页码 1949-1952出版社
SPRINGER
DOI: 10.1023/B:BILE.0000003992.09492.4b
关键词
Chinese Hamster Ovary cells; matrix metalloprotease-9; secreted proteases; serum-free medium; zymography
The protease activity secreted by the Chinese Hamster Ovary (CHO-K1) cell line grown in serum-free medium was examined by substrate gel electrophoresis (zymography). The cell line expressed extracellular proteases that were active on gelatin zymograms but not on casein zymograms. The main protease band visible by gelatin zymography was approx. 92 kDa. Incubation of the conditioned medium with aminophenylmercuric acetate (APMA) resulted in the appearance of gelatinase activity at 82 kDa. Incubation of the conditioned media with EDTA significantly decreased the gelatinolytic activity of both the 92 kDa and 82 kDa forms, indicating the gelatinase responsible was a metalloprotease. Immunoblotting of the conditioned medium showed the gelatinase to be the pro-form of matrix metalloprotease-9 (pro-MMP-9), also known as gelatinase B.
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