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  • 1
    Electronic Resource
    Electronic Resource
    Ultrasonography gives directly but noninvasively elastic characteristic of human tendon in vivo (1995)
    Springer
    European journal of applied physiology 71 (1995), S. 555-557 
    Details
    ISSN: 1439-6327
    Keywords: Human tendon elasticity ; Ultrasonography ; Tibialis anterior muscle ; F-L curve
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00238560
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    The protease from Vibrio Cholerae nicks arginine at position 192 from the N-terminus of the heat-labile enterotoxin a subunit from enterotoxigenic Escherichia Coli (1992)
    Springer
    European journal of epidemiology 8 (1992), S. 743-747 
    Details
    ISSN: 1573-7284
    Keywords: EnterotoxigenicEscherichia coli ; Yibrio cholerae ; LT ; CT
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00145394
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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