Frequency of the 35delG allele causing nonsyndromic recessive deafness in the Algerian patients.

Deafness is a heterogeneous disorder showing different patterns of inheritance and involving a multitude of different genes. Mutations in the GJB2 gene encoding connexin 26 (Cx26) protein are a major cause for non-syndromic autosomal recessive and sporadic deafness. Among these mutations, the c.35delG deletion is the most common mutation for sensorineural deafness. One hundred sixteen persons from fifty-eight families were tested by the method based on the principle of PCR-mediated-site-directed mutagenesis (PSDM), followed by a Bsl1 digestion. Mutation c.35delG was diagnosed in sixteen families (11 homozygotes and 5 heterozygotes). The low allelic frequency (17.24%) and low ratio of individuals homozygous (13.8%) and heterozygous (6.9%) for the c.35delG mutation suggest that there are other mutations in the GJB2 gene or other genes responsible for deafness in the Algerian population. This study reports a significant association (P=0.003) between first cousin consanguinity and non-syndromic prelingual deafness.

[Differential spirometry and computerized pulmonary ventilation- perfusion scintiphotography as preoperative functional studies in thoracic surgery]. / La spirometria separata e la scintifotografia polmonare perfusoria e ventilatoria computerizzata quali indagini funzionali pre-operatorie in chirurgia toracica.

With purposes of a better knowledge of the respiratory function, and for a more and more exact postoperative functional prognosis, the authors considered the results obtained by the differential bronchospirometry and the pulmonary ventilation-perfusion imaging. Through the study of 10 patients, susceptible of operations for lung extirpation, they could so evaluate the reliability and usefulness of said two functional investigations, which can integrate and complete each other.

Polyclonal antibodies against iduronate 2-sulphate sulphatase from human urine.

Human iduronate 2-sulphate sulphatase (EC 3.1.6.-) from urine has been purified by affinity chromatography on concanavalin A-Sepharose, ammonium sulphate fractionation and DEAE-cellulose chromatography. With ion-exchange chromatography, the enzyme was resolved in two activity peaks. The less anionic of these forms was further purified by polyacrylamide gel electrophoresis under non-denaturing conditions. Anti-iduronate 2-sulphate sulphatase antibodies were obtained from mice immunized with polyacrylamide eluted enzyme. The specificity of the antibodies towards iduronate 2-sulphate sulphatase was demonstrated by immunoprecipitation of the enzyme from partially purified urine protein. The procedure described in this work opens the way to the application of hybridoma technology to iduronate 2-sulphate sulphatase.