Publications (6)51.03 Total impact

  • J Peters · D M Swallow · S J Andrews · L Evans
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    ABSTRACT: An electrophoretically detectable variant of acid α-glucosidase has been found in SM/J mice. This variant is attributable to excess sialylation of the enzyme and is determined by a gene, alpha-glucosidase processing, Aglp, on chromosome 17. In addition, as also reported by Potier, Lu Shun Yan & Womack (1979), SM/J mice are relatively deficient in neuraminidase and it appears that the low level of this enzyme in SM/J is determined by an autosomal codominant gene, neuraminidase-1, Neu-1. Preliminary data indicate that Neu-1 is also on chromosome 17. It seems probable that the several processing genes Apl, Aglp and Map-2 which are all closely linked on chromosome 17 are one and the same, a gene Neu-1 coding for neuraminidase.
    No preview · Article · Sep 1981 · Genetics Research
  • [Show abstract] [Hide abstract]
    ABSTRACT: An electrophoretically detectable variant of acid α-glucosidase has been found in SM/J mice. This variant is attributable to excess sialylation of the enzyme and is determined by a gene, alpha-glucosidase processing, Aglp, on chromosome 17. In addition, as also reported by Potier, Lu Shun Yan & Womack (1979), SM/J mice are relatively deficient in neuraminidase and it appears that the low level of this enzyme in SM/J is determined by an autosomal codominant gene, neuraminidase-1, Neu-1. Preliminary data indicate that Neu-1 is also on chromosome 17. It seems probable that the several processing genes Apl, Aglp and Map-2 which are all closely linked on chromosome 17 are one and the same, a gene Neu-1 coding for neuraminidase.
    No preview · Article · Aug 1981 · Genetics Research
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    ABSTRACT: Observations have been made on two brothers who had progressive ataxia, intention myoclonus and visual failure starting early in the third decade of life. Their parents were consanguineous. The brothers showed bilateral cherry red spots at the maculae and bilateral perinuclear cataracts; their intelligence was preserved. Urine was found to contain large amounts of sialylated oligosaccharides; cultured skin fibroblasts showed deficiency of the enzyme sialidase (neuraminidase). Studies on leucocytes and cultured skin fibroblasts showed aberrant electrophoretic mobilities of six enzymes all of which are known to be glycoproteins, and this has been attributed to excessive amounts of sialic acid on the enzyme molecules. The clinical features together with the biochemical findings indicate that these are further cases of the newly described condition Sialidosis Type 1 and it is suggested that the electrophoretic findings might be typical of the condition.
    Full-text · Article · Aug 1979 · Annals of Human Genetics
  • E Solomon · D Swallow · S Burgess · L Evans
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    ABSTRACT: Hybrid clones (MOGs) were made between the mouse line RAG and a primary fibroblast line from an individual of the rare alphaGLU 2 phenotype. Fifteen independent primary clones and 32 subclones were tested for the presence of human alphaGLU after separation of the human and rodent enzymes by starch gel electrophoresis. Twenty-three other human-mouse hybrids from six different crosses were analysed for the presence of human alphaGLU by exploiting a difference in the thermostability of the human and mouse enzymes. The hybrids were also analysed for up to 25 other enzymes which were used as markers for different human chromosomes. Two of the MOG hybrids were karyotyped and karyotype data were already available for a number of the other hybrids. The combined results demonstrate that alphaGLU is located on chromosome 17, and probably on 17q.
    No preview · Article · Feb 1979 · Annals of Human Genetics
  • Dallas M. Swallow · Lorraine Evans · D A Hopkinson
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    ABSTRACT: THE basis for the complex multiple molecular forms (isozymes) of the enzyme adenosine deaminase (ADA) has been widely studied. The ADA found in human erythrocytes (so-called `red cell' ADA) exhibits genetically determined polymorphism detectable by electrophoresis1, has reactive thiol groups2 and has a low molecular size3.`Red cell' ADA is present in various tissues other than the red cell3, but additional adenosine deaminases. the so-called tissue ADA isozymes a, b, c, d and e named in order of decreasing electrophoretic mobility, which exhibit rather different properties. occur in varying amounts in nonerythroid tissues. With the discovery that the deficiency of `red cell' ADA in certain patients with combined immune deficiency disease is accompanied by the deficiency of all the other isozymes4-6. it became clear that all the forms were probably coded by a single ADA locus. The `red cell' ADA can be converted into the characteristic `tissue' isozymes by tissue extracts both from normal individuals7,8 and from patients with combined immune deficiency disease. A converting factor has been isolated and partially purified and is thought to be a protein9. This protein is presumably associated with one or several `red cell' ADA molecules to form the `tissue' isozymes, accounting for the alteration in properties (increase in molecular size, loss of detectable genetically determined electrophoretic variation and loss of thiol reactivity3). We present here evidence, from lectin affinity chromatography and experiments with neuraminidase. that most of the multiple forms of `tissue' ADA are glycoproteins which differ in their accessible sugar residues. This suggests that the converting factor may be a single glycoprotein with heterogenous carbohydrate content.
    No preview · Article · Oct 1977 · Nature
  • D M Swallow · L Evans · N Saha · H Harris
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    ABSTRACT: 1. An electrophoretic system in which N-acetyl hexosaminidase C (HEX(C)) MIGRATES LESS ANODALLY THAN N-acetyl hexosaminidase A (HEX(A)) is described. 2. HEX(C) is shown to differ from HEX(A) and HEX(B) in substrate specificity, molecular size and affinity for Concanavalin-A. 3. HEX(C) is present in a wide range of adult and foetal tissues and in tissues from patients with Tay-Sachs and Sandhoff's diseases. It is particularly prominent in brain, testis, thymus and lymphoblastoid cell extracts and in several foetal tissues. 4. It is suggested that HEX(C) is coded at a separate gene locus from HEX(A) and HEX(B).
    No preview · Article · Aug 1976 · Annals of Human Genetics