Partial characterization of human collagen and procollagen secreted by human corneal stromal fibroblasts in cell culture.
Human corneal stromal fibroblasts were established into cell culture. Fractions highly enriched for collagen and procollagen were purified from the medium and cell layer. Analysis using polyacrylamide gel electrophoresis and DEAE cellulose chromatography indicated the presence of a heterogeneous population of procollagen molecules ranging in molecular weights from 200,000 to 120,000 daltons along with alpha1 and alpha2 collagen chains. Cyanogen bromide peptides of a corneal peptide fraction migrated concomitantly with type I standard cyanogen bromide peptides.
D002478:Cells, Cultured; D003094:Collagen / Q000032:analysis / Q000096:biosynthesis*; D003315:Cornea / Q000166:cytology*; D005347:Fibroblasts / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008970:Molecular Weight; D010455:Peptides / Q000032:analysis; D011347:Procollagen / Q000032:analysis / Q000096:biosynthesis*
D010455:Peptides; D011347:Procollagen; D003094:Collagen