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  • Characterisation 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.

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Research Article
Characterisation 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.
  1. A J Richards,
  2. J C Lloyd,
  3. P N Ward,
  4. A De Paepe,
  5. P Narcisi,
  6. F M Pope
  1. Dermatology Research Group, Clinical Research Centre, Northwick Park Hospital, Harrow, Middlesex.

    Abstract

    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.

    https://doi.org/10.1136/jmg.28.7.458

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