about infrasound of of α crystal protein molecular chaperone activity(对次声的α晶蛋白质分子伴侣蛋白的活动).docVIP
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about infrasound of of α crystal protein molecular chaperone activity(对次声的α晶蛋白质分子伴侣蛋白的活动)
About infrasound of of α crystal protein molecular chaperone activity
[Keywords:], molecular chaperones Keywords: @ - crystal protein; chaperone; infrasound Abstract: Objective To investigate the infrasound @ - crystal protein molecular chaperone activity. Methods Sephacryl S-300 gel column separation of bovine α-crystallin protein. Applications infrasound pressure cabin, 16Hz, 130dB infrasound @ L - crystal protein solution (g · L-1, daily role 2h, for 16d. spectrophotometer 360nm when @ L - crystal proteins induced by the heating catalase (CAT βL - the protective effect of crystal protein aggregation incubated for 60min to @ L - crystal protein accounted for a percentage of the value of the control target protein light scattering @ - crystal protein chaperone function. Results Compared with control protein compared @ - crystal protein-specific protection CAT and βL - the role of the crystal protein heat coagulation. infrasound the 16th the control group _AT_ L - crystal protein protection βL - crystal protein heat coagulation (92.0 + -3.1%, the infrasound group (81.2 + -5.4)%, decreased by approximately 10.8% (P lt;0.01 ; conclusions of the control group @ L - the crystal proteins protect CAT thermal role of cohesion (73.8 + -5.1%, the infrasound group (61.8 + -9.1%, decreased by approximately 12.0% (P lt;0.01. infrasound can affect @ - Crystals the molecular chaperone activity of the protein.
Keywords: @-crystallin; molecular chaperone; infrasound
Abstract: AIM To investigate the effect of infrasound on molecular chaperone activity of@-crystallin.METHODS The @-crystallin of bovine lens were separated by chromatog-raphy on Sephacryl S-300HR.The solutions of @ L-crystallin (mg ?ml- 1 from nucleus were exposed to infrasound of16Hz with the i ntensity of160dB (2hours per day for16con-secutive days.The protective effects of @ L-crystallin on ther-mal aggregation of catalase andβL-crystallin were measured spectrophotometrically at360nm.The chaperone activi
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