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  • 1985-1989  (2)
  • Bombyx mori  (1)
  • Lysosomal enzymes  (1)
  • Nemaline myopathy  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Molecular cloning of the fibroin light chain complementary DNA and its use in the study of the expression of the light chain gene in the posterior silk gland ofBombyx mori (1985)
    Springer
    Cellular and molecular life sciences 41 (1985), S. 1167-1171 
    Details
    ISSN: 1420-9071
    Keywords: Silkworm ; Bombyx mori ; silk gland ; mRNA ; complementary DNA ; fibroin light chain ; molecular cloning
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Fibroin light chain (L-chain) mRNA (mol. wt 4.0×105 daltons) was purified from the posterior silk gland of the silkworm,Bombyx mori (J-131 strain). Double-stranded complementary DNA was synthesized and inserted into the PstI site of pBR322 employing the oligo(dC)-oligo(dG) tailing method. Several recombinant plasmids containing the inserts of about 800 base pairs were isolated. Hybridization-translation assay demonstrated that these clones hybridized specifically with the fibroin L-chain mRNA. One of these clones (pLA23) was used as a probe to investigate relative concentrations of the fibroin L-chain gene and mRNA in the posterior silk glands at different stages of late larval development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01951711
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Progression in nemaline myopathy (1989)
    Springer
    Acta neuropathologica 78 (1989), S. 484-491 
    Details
    ISSN: 1432-0533
    Keywords: Nemaline myopathy ; Lysosomal enzymes ; Acid phosphatase ; Cathepsins ; Myofibrillar degeneration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Four of seven patients with nemaline myopathy had severe, rapidly progressing symptoms. These four showed an increase in acid phosphatase activity in muscle fibers demonstrated by histochemistry and cathepsin B&L activity by biochemical measurement. On electron microscopy, nemaline bodies, occasionally disorganized myofibrils and autophagic vacuoles containing sarcoplasmic debris and glycogen particles were seen. Focal myofibrillar degeneration, through an unknown pathogenetic mechanism, induces an increase in lysosomal enzymes in the skeletal muscles which may be closely correlated with a rapid aggravation of muscle weakness in nemaline myopathy.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00687709
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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