Literature DB >> 2757356

Screening for thermostability and electrophoretic red blood cell sorbitol dehydrogenase (E.C.1.1.1.14) variants.

B Ibarra1, G Vaca, F J Perea, M Rábago, C Alvarez, C Ortíz, C Medina.   

Abstract

A screening for both thermostability and electrophoretic red blood cell sorbitol dehydrogenase (RBC-SORD) variants in blood donors was performed. SORD activity in standard conditions (unheated samples) in 274 individuals was 198 +/- 38.6 mIU/g Hb. The ratio of enzymatic activity after heating (H) to the activity in controls (C) before heating (H/C ratio) was 0.39 +/- 0.10. H/C ratios minor than 0.1 in 3 out of 274 blood donors and higher than 0.9 in 1 were observed. In 208 individuals, four electrophoretic phenotypes were observed: I) Three bands, named a, b and c, with cathodic mobility in 163 individuals (78.36%); II) Two bands a and c in 25 individuals (12.02%); III) Two bands b and c in 14 (6.73%); and IV) One band, c in 6 (2.88%). Studies carried out to characterize the three bands suggest that they are isozymes of the same locus with the observation of an interchange of the bands as a normal phenomena.

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Year:  1989        PMID: 2757356

Source DB:  PubMed          Journal:  Ann Genet        ISSN: 0003-3995


  1 in total

1.  Membrane-bound sorbitol dehydrogenase in human red blood cells. Studies in normal subjects and in enzyme-deficient subjects with congenital cataracts.

Authors:  A Alvarez; A Martínez; B Ibarra; C Medina; M Bracamontes; J Perea; G Vaca
Journal:  J Inherit Metab Dis       Date:  1993       Impact factor: 4.982

  1 in total

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