Folding and activity of recombinant human procollagen C‐proteinase enhancer
作者： Laura Moschcovich , Simonetta Bernocco , Bernard Font , Hadassah Rivkin , Denise Eichenberger
DOI: 10.1046/J.1432-1327.2001.02189.X
关键词:
摘要: Recombinant human procollagen C-proteinase enhancer (rPCPE) was expressed using a baculovirus system and purified to homogeneity three-step procedure including heparin affinity chromatography. Heparin binding dependent on the C-terminal netrin-like domain. The recombinant protein found be active, increasing activity of C-proteinase/bone morphogenetic protein-1 type I in manner comparable native protein. Enhancing intact disulfide bonding within By circular dichroism, observed secondary structure rPCPE consistent with known three-dimensional structures proteins containing homologous domains.
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