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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Acta neuropathologica 19 (1971), S. 51-69 
    ISSN: 1432-0533
    Keywords: Human Skeletal Muscle ; Autopsy Material ; Biometric Analysis ; Fiber Diameter ; Histograms
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary This study represents an effort to tabulate the normal mean cross-sectional diameters of human striated muscle fibers in post-mortem material ranging in age from five months gestation through senescence. Age, sex, height and weight of the subjects were taken into account. Cases with neuromuscular illnesses or inanition were specifically excluded. All measurements represent mean narrow fiber diameter of celloidin embedded material sampled at the maximum diameter of the muscle belly. Noteworthy findings include a rapid increase in mean narrow diameter of all muscles except gastrocnemius from gestation to the immediate neonatal period. This was followed by a slower gradual increase in fiber diameter until the age of puberty when again a rapid increase was noted in all muscles except the superior rectus. Following puberty, the superior rectus diameter remained relatively constant throughout life. The sternomastoid, deltoid, biceps, sartorius, quadriceps and gastrocnemius continued a gradual steady increase in fiber size until the late third to early fourth decade, thereafter slowly diminishing in size by the ninth decade. Data are presented to show that the fusiform shape of the biceps muscle cannot be entirely attributed to the fusiform shape of the individual fibers. Particular care must be taken in selecting the level of measurement as fiber diameters appear to be significantly larger near the maximum breadth of the muscle bely. Factors are presented for conversion of measurements between various methods of histologic processing. A useful rule is that the ratio of the sizes of fresh-frozen, fixed-frozen, celloidin and paraffin embedded fibers is roughly 10:9:8:7.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Key words Restriction endonuclease ; Methylase selection ; Gene expression ; DNA methylation ; Recombinant DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The genes encoding the ApaLI (5′-G^TGCAC-3′), NspI (5′-RCATG^Y-3′), NspHI (5′-RCATG^Y-3′), SacI (5′-GAGCT^C-3′), SapI (5′-GCTCTTCN1^-3′, 5′-^N4GAAGAGC-3′) and ScaI (5′-AGT^ACT-3′) restriction-modification systems have been cloned in E.␣coli. Amino acid sequence comparison of M.ApaLI, M.NspI, M.NspHI, and M.SacI with known methylases indicated that they contain the ten conserved motifs characteristic of C5 cytosine methylases. NspI and NspHI restriction-modification systems are highly homologous in amino acid sequence. The C-termini of the NspI and NlaIII (5′-CATG-3′) restriction endonucleases share significant similarity. 5mC modification of the internal C in a SacI site renders it resistant to SacI digestion. External 5mC modification of a SacI site has no effect on SacI digestion. N4mC modification of the second base in the sequence 5′-GCTCTTC-3′ blocks SapI digestion. N4mC modification of the other cytosines in the SapI site does not affect SapI digestion. N4mC modification of ScaI site blocks ScaI digetion. A DNA invertase homolog was found adjacent to the ApaLI restriction-modification system. A DNA transposase subunit homolog was found upstream of the SapI restriction endonuclease gene.
    Type of Medium: Electronic Resource
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