An account of two new ICD‐S variants not detectable in red blood cells

Turner, Bryan M.; Fisher, Rachel; Garthwaite, Elizabeth; Whale, R. J.; Harris, Harry

doi:10.1111/j.1469-1809.1974.tb01851.x

Cited by 7 publications

(2 citation statements)

References 9 publications

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“…According to this hypothesis, such mutant gene expression and the existence of a putative "hybrid" dimer are not seen in erythrocytes because this labile protein species is degraded too rapidly. Molecular variants of peptidase A (Sinka et al, 1970;Lewis, 1973), isocitrate dehydrogenase (Turner et al, 1973), and peptidase C (Povey et al, 1972) are other examples where mutant gene expression is observed in other tissues but not in erythrocytes, presumably for the reason noted above. Alternately, the higher levels of activity and CRM found in cultured lymphoblasts may be due to a compensatory mechanism in the cell which increases the expression of the normal allele, while either the mutant allele is not expressed or its product is labile and undetectable by these assays.…”

Section: Discussionmentioning

confidence: 99%

Human adenine phosphoribosyltransferase: Characterization from subjects with a deficiency of enzyme activity

et al. 1983

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Adenine phosphoribosyltransferase (APRT) was characterized with respect to specific activity and immunoreactive protein (CRM) levels in hemolysate from 18 members of an APRT-deficient kindred. In addition, lymphoblastoid cell lines were established from six of these subjects and APRT from these cells was characterized in a similar fashion. Levels of specific activity and CRM in patients homozygous for the deficiency were less than 1% of normal. Heterozygous subjects had higher levels of activity and CRM in lymphoblasts than in erythrocytes and, in all cases, the APRT present was normal in terms of isoelectric point, subunit molecular weight, and heart stability. The higher levels of activity and CRM found in lymphoblasts may be due either to expression of a mutant gene product stabilized in a normal:mutant dimer or to autologous regulation.

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Section: Discussionmentioning

confidence: 99%

Human adenine phosphoribosyltransferase: Characterization from subjects with a deficiency of enzyme activity

et al. 1983

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“…The finding of small positive lod scores with IDH, is of interest since this locus, like ACP,, has been assigned to chromosome 2 (Creagan et al 1974). Variation at this locus is uncommon, but of the families with IDH, variants described from this laboratory (Turner et al 1974), two are informative for ACP,. The pedigrees are given in Figs.…”

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confidence: 81%

Linkage data on red cell acid phosphatase from family studies

Mace

Cook

Robson

1975

Annals of Human Genetics

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Probable assignment of soluble isocitrate dehydrogenase (IDH1) to 2q33.3

et al. 1985

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Gene dosage effects for soluble isocitrate dehydrogenase (IDH1) were investigated in four unrelated cases with abnormalities involving the long arm of chromosome 2. Case 1 was trisomic for 2q33.3----qter, Case 2 monosomic for 2q33.3----q35, Case 3 trisomic for 2q11.2----q24.2, and Case 4 monosomic for 2q23----q24.2. These abnormalities were de novo except in Case 1, where trisomy 2q resulted from a maternal translocation. The red cell IDH1 levels were significantly reduced in Cases 1 (41.4% of normal value) and 2 (51.9%), while they were normal in Cases 3 and 4. The low IDH1 level also in the father of Case 1 (43.6%), together with the common electrophoretic phenotype of IDH1 in red cells as well as leukocytes, led us to suppose that Case 1 was really heterozygous for common and probable null alleles, and that the IDH1 gene locus could be excluded from 2q33.3----qter. On the other hand, normal IDH1 values in the parents of Case 2 were consistent with the hemizygosity for this locus in Case 2. The results suggested that the IDH1 locus could be assigned to the 2q33.3 band, especially the proximal portion of it.

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An account of two new ICD‐S variants not detectable in red blood cells

Cited by 7 publications

References 9 publications

Human adenine phosphoribosyltransferase: Characterization from subjects with a deficiency of enzyme activity

Human adenine phosphoribosyltransferase: Characterization from subjects with a deficiency of enzyme activity

Linkage data on red cell acid phosphatase from family studies

Probable assignment of soluble isocitrate dehydrogenase (IDH1) to 2q33.3

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