Characterization of human type III collagen expressed in a baculovirus system. Production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit

An efficient expression system for recombinant collagens would have numerous scientific and practical applications. Nevertheless, most recombinant systems are not suitable for this purpose, as they do not have sufficient amounts of prolyl 4-hydroxylase activity. Pro-alpha 1 chains of human type III...

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Bibliographic Details

Published in:	The Journal of biological chemistry Vol. 271; no. 20; pp. 11988 - 11995
Main Authors:	Lamberg, A, Helaakoski, T, Myllyharju, J, Peltonen, S, Notbohm, H, Pihlajaniemi, T, Kivirikko, K I
Format:	Journal Article
Language:	English
Published:	United States 17-05-1996
Subjects:	Animals Baculoviridae - genetics Humans Procollagen - biosynthesis Procollagen - chemistry Procollagen - isolation & purification Procollagen-Proline Dioxygenase - biosynthesis Protein Conformation Recombinant Proteins - biosynthesis Spodoptera
Online Access:	Get full text
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