Gesierich U, Pfeil W
University of Potsdom, Max-Delbrück-Centre for Molecular Medicine, Berlin-Buch, Germany.
FEBS Lett. 1996 Sep 16;393(2-3):151-4. doi: 10.1016/0014-5793(96)00867-8.
The eye lens protein and chaperonin, alpha-crystallin, was studied by differential scanning microcalorimetry, spectroscopy and size exclusion chromatography. The thermal transition of alpha-crystallin proceeds at Ttrs = 59.8 +/- 0.6 degrees C with an enthalpy change of delta H = 336 +/- 9 kJ per mol subunit. Disagreement between previous delta H values could be attributed to a side reaction that leads, depending on the scan rate, to the formation of a non-productive folding form. The conformational stability of alpha-crystallin is rather low (delta G = 24 +/- 5 kJ/mol of subunit). The minimal cooperative unit of alpha-crystallin is the monomeric subunit.
通过差示扫描量热法、光谱法和尺寸排阻色谱法对眼晶状体蛋白和伴侣蛋白α-晶状体蛋白进行了研究。α-晶状体蛋白的热转变在Ttrs = 59.8±0.6℃下进行，每摩尔亚基的焓变为ΔH = 336±9 kJ。先前ΔH值之间的差异可归因于一种副反应，该副反应根据扫描速率导致形成非生产性折叠形式。α-晶状体蛋白的构象稳定性相当低（ΔG = 24±5 kJ/mol亚基）。α-晶状体蛋白的最小协同单位是单体亚基。
