The application of a pulse eddy current process for the non-destructive testing of austenitic pipes damaged by corrosion (in German) : 39926 Wittig, G.; Thomas, H.M.; Maser, D.; Hennig, P.; Weigelt, G. Bundensanstalt fuer Material Prufung, Berlin (FDR), TIB/B88-81343/GAR, 97 pp. (Dec. 1986)

Abstract

Two missense mutations in exon 6 of the LPL gene were identified on separate alleles in a Dutch patient with lipoprotein lipase (LPL) deficiency. The first mutation is a G1003 → A transition resulting in a D250N mutation, which has been shown previously to result in a catalytically defective protein in patients of French-Canadian ancestry. The second mutation, a C to G transition at nucleotide 1007, predicts a S251C residue change in the highly conserved region of LPL surrounding the loop structure that covers the catalytic triad. This mutation constitutes a novel defect among LPL gene mutations reported so far. Site-directed mutagenesis experiments provide in-vitro evidence for the complete loss of LPL activity resulting from this latter missense mutation. The G1003 → A nucleotide substitution underlying the Asp250 mutation deletes a TaqI endonuclease recognition site and the C1007 → G change that leads to the S251C alteration abolishes a HinfI recognition site. This will facilitate rapid screening for these mutations in LPL-deficient patients.