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Folding and activity of recombinant human procollagen C-proteinase enhancer
Year:
2001
Source of publication :
European Journal of Biochemistry
Authors :
Chejanovsky, Nor
;
.
Rivkin, Hadassah
;
.
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
Facilitators :
From page:
2991
To page:
2996
(
Total pages:
6
)
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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More details
DOI :
10.1046/j.1432-1327.2001.02189.x
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
28327
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:38
Scientific Publication
Folding and activity of recombinant human procollagen C-proteinase enhancer
268
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
Folding and activity of recombinant human procollagen C-proteinase enhancer
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.
Scientific Publication
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