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  • 1985-1989  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Mutation in GM2-Gangliosidosis B1 Variant (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 50 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Fibroblasts from a patient with GM2-gangliosidosis B1 variant contained mRNA of normal size but in reduced quantity for the β-hexosaminidase α subunit. The nucleotide sequence of a cDNA clone that included the entire protein coding sequence was completely normal except for a sinde base substitution from G to A at no. 533, resulting in a change from arginine to histidine at amino acid no. 178. The same mutation was found in two other cDNA clones. The position of the mutation is ∼90 amino acids from the N-terminus of the mature, processed enzyme. Computer analysis predicated substantial alterations in the secondary structure of the enzyme protein. These results provide new insight into functional domains of this enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb13266.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A Point Mutation in the Coding Sequence of the β-Hexosaminidase α Gene Results in Defective Processing of the Enzyme Protein in an Unusual GM2-Gangliosidosis Variant (1988)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 51 (1988), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: cDNA clones were isolated from cultured fibro-blasts of a patient previously reported as having GM2-gangliosidosis due to defective processing of the precursor β-hexosaminidase α chain. Sequence analysis of a clone containing the entire protein coding sequence showed a single nucleotide substitution, from G to A, at nucleotide residue no. 1444, which resulted in a change in amino acid residue no. 482, from the normal glutamic acid to lysine. This transversion was confirmed in two other cDNAs from the same unamplified library. The results collectively indicate that the change from the strongly negative to strongly positive charge at amino acid residue no. 482 is responsible for the defective processing of the enzyme in this patient.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1988.tb01836.x
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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