Characterization of an arginine 789 to cysteine substitution in alpha 1 (II) collagen chains of a patient with spondyloepiphyseal dysplasia
D Chan, TK Taylor, WG Cole - Journal of Biological Chemistry, 1993 - ASBMB
A child with spondyloepiphyseal dysplasia congenita was shown to be heterozygous for a
mutation of the COL2A1 gene that encodes the alpha 1 (II) chain of type II collagen. The
alpha 1 (II) chains extracted from cartilage contained disulfide-bonded dimeric and trimeric
alpha 1 (II) chains. Carboxymethylation confirmed that some of the type II collagen chains
contained cysteine residues that are not normally present in alpha 1 (II) chains. Cyanogen
bromide peptide mapping showed that the abnormal cysteine residue was located in the …
mutation of the COL2A1 gene that encodes the alpha 1 (II) chain of type II collagen. The
alpha 1 (II) chains extracted from cartilage contained disulfide-bonded dimeric and trimeric
alpha 1 (II) chains. Carboxymethylation confirmed that some of the type II collagen chains
contained cysteine residues that are not normally present in alpha 1 (II) chains. Cyanogen
bromide peptide mapping showed that the abnormal cysteine residue was located in the …