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  • Fiber Diameter  (1)
  • Gene expression  (1)
  • aluminum  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    The journal of membrane biology 99 (1987), S. 187-196 
    ISSN: 1432-1424
    Schlagwort(e): membrane ; aluminum ; channel ; mitocondrion ; voltage dependence ; VDAC
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie
    Notizen: Summary The mitochondrial outer membrane contains voltagegated channels called VDAC that are responsible for the flux of metabolic substrates and metal ions across this membrane. The addition of micromolar quantities of aluminum chloride to phospholipid membranes containing VDAC channels greatly inhibits the voltage dependence of the channels' permeability. The channels remain in their high conducting (open) state even at high membrane potentials. An analysis of the change in the voltage-dependence parameters revealed that the steepness of the voltage dependence decreased while the voltage needed to close half the channels increased. The energy difference between the open and closed states in the absence of an applied potential did not change. Therefore, the results are consistent with aluminum neutralizing the voltage sensor of the channel. pH shift experiments showed that positively charged aluminum species in solution were not involved. The active form was identified as being either (or both) the aluminum hydroxide or the tetrahydroxoaluminate form. Both of these could reasonably be expected to neutralize a positively charged voltage sensor. Aluminum had no detectable effect of either single-channel conductance or selectivity, indicating that the sensor is probably not located in the channel proper and is distinct from the selectivity filter.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Acta neuropathologica 19 (1971), S. 51-69 
    ISSN: 1432-0533
    Schlagwort(e): Human Skeletal Muscle ; Autopsy Material ; Biometric Analysis ; Fiber Diameter ; Histograms
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: 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.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 1617-4623
    Schlagwort(e): Key words Restriction endonuclease ; Methylase selection ; Gene expression ; DNA methylation ; Recombinant DNA
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: 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.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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