作者: Micky D. Tortorella , Elizabeth C. Arner , Robert Hills , Jennifer Gormley , Kam Fok
DOI: 10.1016/J.ABB.2005.09.018
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摘要: Abstract ADAMTS-4 (aggrecanase 1) is synthesized as a latent precursor protein that may require activation through removal of its prodomain before it can exert catalytic activity. We examined various proteinases well auto-activation under wide range conditions for the and induction enzymatic The proprotein convertases, furin, PACE4, PC5/6 efficiently removed cleavage at Arg 212 /Phe 213 , generating an active enzyme. Of broad proteases evaluated, only MMP-9 trypsin were capable removing prodomain. In presence mercuric compounds, autocatalysis was not observed, nor observed temperatures from 22 to 65 °C, ionic strengths 0.1 1 M, or acidic/neutral pH. At basic pH 8–10, by occurred, conclusion, pro-form catalytically limited number mechanisms mediate N-terminal activation.