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  • 1
    Digitale Medien
    Digitale Medien
    Springer
    European journal of applied physiology 71 (1995), S. 555-557 
    ISSN: 1439-6327
    Schlagwort(e): Human tendon elasticity ; Ultrasonography ; Tibialis anterior muscle ; F-L curve
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract To obtain an insight into tendon elasticity during human movement, a real-time ultrasonography was applied to the contracting tibialis anterior muscle. The insertion point of fascicles onto the aponeurosis was clearly visualized, and its position relative to a fixed marker on the skin moved proximally (Δ1) according to the increasing dorsiflexion force (ΔF) with a fixed ankle joint. Notably, the Δ1 − ΔF relationship in the tendon was found to be quadratic in nature (ΔF = cΔ12; c=1.48 ∼ 2.24, r=0.985 ∼ 0.992, n=9) as has been reported in the isolated tendon, although the ΔF − Δ1 curves were slightly underestimated in comparison with the stiffness constant estimated from tendon architecture. This underestimation might be caused by changes in the height of the foot arch with the application of force.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1573-7284
    Schlagwort(e): EnterotoxigenicEscherichia coli ; Yibrio cholerae ; LT ; CT
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract It was examined where a protease purified from Vibrio cholerae might nick the heat-labile enterotoxin (LT) A subunit from enterotoxigenicEscherichia coli. LT was digested by the protease and contained a fragment which had the same mobility on SDS-PAGE as that of the Al fragment of LT digested by trypsin. The biological activity of LT by this protease was also identical to that of LT by trypsin. The amino acid sequence of the N-terminus of the A2-like fragment was Thr-Ser-Thr-Gly, which corresponded to the sequence from 193 to 196 of the A subunit. These data suggest that this protease, like trypsin, nicks arginine at position 192 from the N-terminus of the A subunit and that the biological activation of LT by this protease is similar to that by trypsin.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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