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Elastic constants and high-temperature elastic anomalies near 425 K in lithium hydrazinium sulfate (1994)

Godfrey, L. ; Philip, J. ; Sebastian, M. T.

[S.l.] : American Institute of Physics (AIP)

Journal of Applied Physics 75 (1994), S. 2393-2397

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ISSN: 1089-7550

Source: AIP Digital Archive

Topics: Physics

Notes: All the nine elastic constants of the orthorhombic crystal lithium hydrazinium sulfate, Li(N2H5)SO4, have been determined by measuring ultrasonic velocities using pulse echo overlap technique at 10 MHz. Temperature variation of all the six diagonal elastic constants and the three off-diagonal combinations have been measured between 300 and 450 K. Some of the constants show anomalous behavior in the 410–440 K temperature region, which is attributed to a phase transition in the crystal near 425 K. Magnitude of the velocity anomaly is comparatively small. A new high-temperature ultrasonic bond material suitable for transverse waves is also reported.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1063/1.356260

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Ca-EGTA affects the relationship between [Ca2+] and tension in α-toxin permeabilized rat anococcygeus smooth muscle (1993)

Smith, Godfrey L. ; Crichton, Catherine A.

Springer

Journal of muscle research and cell motility 14 (1993), S. 76-84

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ISSN: 1573-2657

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Medicine

Notes: Summary The relationship between calcium concentration ([Ca2+]) and force in smooth muscle can be studied by permeabilizing the sarcolemma and bathing the preparation in a mock intracellular solution. Normally [Ca2+] is set in these solutions using the Ca2+ chelator EGTA in the concentration range of 4–10 mm. This study shows that lowering total EGTA concentration ([EGTA]t) below 10 mm depresses Ca2+-activated force generated in 0.1 μm Ca2+. The observed threshold for the effect of EGTAt is 0.2 mm, and the effect is maximal at approximately 10 mm. BAPTA, another Ca2+ chelator, also produces this effect. Tension production in smooth muscle is controlled by acto-myosin interaction. This in turn is mediated by the relative activities of myosin light chain kinase (MLCK) and phosphatase (MLCP). Inhibiting MLCP with Microcystin LR (10 μm), an increase [EGTAt] from 0.2 mm to 10 mm still enhanced force. This suggests that EGTA promotes phosphorylation of myosin by the activation of MLCK and not by inhibition of MLCP.