Article
Self-assembly of collagen I from a proband homozygous for a mutation that substituted serine for glycine at position 661 in the alpha 2(I) chain. Possible relationship between the effects of mutations on critical concentration and the severity of the phenotype.
The Journal of biological chemistry - 15 Apr 1994
Romanic A M, Spotila L D, Adachi E, Engel J, Hojima Y, Prockop D J
Abstract excerpt
Procollagen I was isolated from cultured skin fibroblasts from a proband who was homozygous for a mutation in the COL1A2 gene that substituted a serine codon for a glycine codon at position 661 of the alpha 2(I) chain. The procollagen I was cleaved to pCcollagen I by procollagen N-proteinase and...
Topics
- Amino Acid Sequence
- Cells, Cultured
- Collagen
- Female
- Fibroblasts
- Glycine
- Humans
- Kinetics
- Macromolecular Substances
- Microscopy, Electron
- Phenotype
- Point Mutation
- Procollagen
- Procollagen N-Endopeptidase