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  • 1
    Electronic Resource
    Electronic Resource
    Carrier detection in ornithine transcarbamylase deficiency (1982)
    Springer
    Journal of inherited metabolic disease 5 (1982), S. 37-40 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We have studied six known heterozygotes for ornithine transcarbamylase (McKusick 31125; OTC) deficiency. All had abnormal results when tested by measurement of urine orotic acid after protein loading. Duodenal mucosa OTC assay detected fewer of the known heterozygotes but was a useful supplementary test. Urine orotic acid excretion after protein loading is influenced by age and results from women being tested must be compared with those from controls of appropriate age.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01799752
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Immunological evidence for a carbamylphosphate synthetase lesion resulting in the formation of enzyme with altered sub-unit size (1986)
    Springer
    Journal of inherited metabolic disease 9 (1986), S. 367-373 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A partial carbamylphosphate synthetase (CPS: EC 6.3.4.16) deficiency (McKusick 23730) was found in a male child who presented with generalized convulsions, rickets and apnoeic attacks at six months of age. By his second year he showed serious developmental delay and a gut biopsy revealed an absence of CPS activity with an elevated ornithine transcarbamylase activity. Analysis of the gut biopsy sample on SDS-polyacrylamide gels, followed by electrophoretic transfer to a nitrocellulose filter probed with monospecific antibodies to CPS showed that the child had normal levels of immunoreactive enzyme, but instead of one band corresponding to normal CPS with a subunit size of 165 000u, the patient had three immunoreactive bands, one larger and two smaller than that found in normal controls. The genetic defect in this child therefore results in an unusual form of CPS being made which has markedly reduced enzyme activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01800486
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    The location of (1→3)-β-glucans in the walls of pollen tubes of Nicotiana alata using a (1→3)-β-glucan-specific monoclonal antibody (1991)
    Springer
    Planta 185 (1991), S. 1-8 
    Details
    ISSN: 1432-2048
    Keywords: Callose ; Cell wall ; (1→3)-β-Glucan ; Nicotiana alata ; Pollen tube ; Monoclonal antibody
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The location of the (1→3)-β-glucan, callose, in the walls of pollen tubes in the style of Nicotiana alata Link et Otto was studied using specific monoclonal antibodies. The antibodies were raised against a laminarinhaemocyanin conjugate. One antibody selected for further characterization was specific for (1→3)-β-glucans and showed no binding activity against either a cellopentaose-bovine serum albumin (BSA) conjugate or a (1→3, 1→4)-β-glucan-BSA conjugate. Binding was inhibited by (1→3)-β-oligoglucosides (DP, 3–6) with maximum competition being shown by laminaripentaose and laminarihexaose, indicating that the epitope included at least five (1→3)-β-linked glucopyranose residues. The monoclonal antibody was determined to have an affinity constant for laminarihexaose of 2.7. 104M−1. When used with a second-stage gold-labelled, rabbit anti-mouse antibody, the monoclonal antibody probe specifically located the (1→3)-β-glucan in the inner wall layer of thin sections of the N. alata pollen tubes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00194507
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
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