CHARACTERIZATION OF A GLYCINE TO VALINE SUBSTITUTION AT AMINO-ACID POSITION-910 OF THE TRIPLE HELICAL REGION OF TYPE-III COLLAGEN IN A PATIENT WITH EHLERS-DANLOS SYNDROME TYPE-IV

We have studied a patient with Ehlers-Danlos syndrome type IV. Protein mapping studies of her type III collagen had indicated that cyanogen bromide fragment 9 contained the site of the mutation. Here we describe the mapping of this region for a single base mutation using a chemical modification and cleavage technique. Sequence analysis of cDNA showed a G to T mutation resulting in the substitution of glycine 910 by valine. This was confirmed by allele specific oligonucleotide hybridisation to the proband's genomic DNA.