TEMPERATURE-INDUCED EXPOSURE OF HYDROPHOBIC SURFACES AND ITS EFFECT ON THE CHAPERONE ACTIVITY OF ALPHA-CRYSTALLIN
TEMPERATURE-INDUCED EXPOSURE OF HYDROPHOBIC SURFACES AND ITS EFFECT ON THE CHAPERONE ACTIVITY OF ALPHA-CRYSTALLIN
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DOI：
10.1016/0014-5793(95)00775-5
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发表时间：
1995-08-07
期刊：
影响因子：
3.5
通讯作者：
SUREWICZ, WK
中科院分区：
文献类型：
--
作者：
DAS, KP;SUREWICZ, WK
α-晶体蛋白是眼晶状体的主要蛋白质，已知与小的热休克蛋白有广泛的相似之处，并充当分子伴侣。用双ANS疏水探针的荧光光谱研究了α-晶体蛋白疏水表面的暴露情况。加热后，蛋白质经历了构象转变，这与表面疏水性的显着增加有关。这种转变发生在大约38摄氏度到50摄氏度之间，缺乏可逆性。表面疏水性的增加与蛋白质伴侣活性的增加有关。这些结果表明疏水相互作用在α-晶状体蛋白的伴侣作用中起主要作用。
alpha-Crystallin, the major protein of the ocular lens, is known to have extensive similarities to small heat shock proteins and to act as a molecular chaperone. The exposure of hydrophobic surfaces on alpha-crystallin was studied by fluorescence spectroscopy using the hydrophobic probe bis-ANS. Upon heating the protein undergoes a conformational transition which is associated with a marked increase in surface hydrophobicity. This transition, which occurs between approximately 38 and 50 degrees C, lacks reversibility. The increase in surface hydrophobicity correlates with the increased chaperone activity of the protein. These results indicate that hydrophobic interactions play a major role in the chaperone action of alpha-crystallin.