אסיף מאגר המחקר החקלאי

Folding and activity of recombinant human procollagen C-proteinase enhancer

Year:

2001

Source of publication :

Authors :

Volume :

268

Co-Authors:

Moschcovich, L., Goldschleger Eye Research Institute, Tel Aviv University Sackler Faculty of Medicine, Sheba Medical Center, Tel Hashomer, Israel
Bernocco, S., Institut de Biologie et Chimie des Protéines, CNRS UMR 5086, Université Claude Bernard Lyon I, Lyon, France
Font, B., Institut de Biologie et Chimie des Protéines, CNRS UMR 5086, Université Claude Bernard Lyon I, Lyon, France
Rivkin, H., Entomology Department, Institute of Plant Protection, Volcani Center, Bet Dagan, Israel
Eichenberger, D., Institut de Biologie et Chimie des Protéines, CNRS UMR 5086, Université Claude Bernard Lyon I, Lyon, France
Chejanovsky, N., Entomology Department, Institute of Plant Protection, Volcani Center, Bet Dagan, Israel
Hulmes, D.J.S., Institut de Biologie et Chimie des Protéines, CNRS UMR 5086, Université Claude Bernard Lyon I, Lyon, France
Kessler, E., Goldschleger Eye Research Institute, Tel Aviv University Sackler Faculty of Medicine, Sheba Medical Center, Tel Hashomer, Israel, Goldschleger Eye Res. Institute, Sheba Medical Center, Tel Hashomer 52621, Israel

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Abstract:

Recombinant human procollagen C-proteinase enhancer (rPCPE) was expressed using a baculovirus system and purified to homogeneity using a three-step procedure including heparin affinity chromatography. Heparin binding was dependent on the C-terminal netrin-like domain. The recombinant protein was found to be active, increasing the activity of procollagen C-proteinase/bone morphogenetic protein-1 on type I procollagen in a manner comparable to the native protein. Enhancing activity was dependent on intact disulfide bonding within the protein. By circular dichroism, the observed secondary structure of rPCPE was consistent with the known three-dimensional structures of proteins containing homologous domains.

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