RADIATION INACTIVATION OF MEMBRANE-PROTEINS - MOLECULAR-WEIGHT ESTIMATES INSITU AND AFTER TRITON-X-100 SOLUBILIZATION
RADIATION INACTIVATION OF MEMBRANE-PROTEINS - MOLECULAR-WEIGHT ESTIMATES INSITU AND AFTER TRITON-X-100 SOLUBILIZATION
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DOI：
10.1016/0003-2697(84)90185-4
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发表时间：
1984-01-01
影响因子：
2.9
通讯作者：
POTIER, M
中科院分区：
文献类型：
--
作者：
BEAUREGARD, G;POTIER, M
Target size analysis by radiation inactivation is widely used for MW determination of membrane enzymes and receptors in situ without the need for prior solubilization or purification. However, since most MW data available in the literature on membrane proteins involve the use of detergents for solubilization, the target sizes of membrane proteins in situ and after solubilization by detergent treatment were compared. Using data from the literature and personal results, 3 different types of behavior of membrane proteins in the presence of detergents were found: uncoupling of subunits (electric eel acetylcholinesterase, placental steroid sulfatase and human nonspecific .beta.-glucosidase); coupling of protein molecules (mouse liver neuraminidase and rat liver insulin receptor regulatory component); and no major change in quaternary structure (rat liver insulin receptor, kidney .gamma.-glutamyltransferase, asialoglycoprotein receptor, insulin degrading enzyme and human leukocyte neuraminidase). For all these proteins, there is a statistically significant increase in target size of about 24% over the value obtained in situ without detergent. A relatively large body of literature data involving a variety of membrane poteins, membrane types and irradiation conditions (electron accelerators or 60Co sources, and proteins irradiated in lyophilized form or frozen solution) was examined, and it was concluded that target sizes of membrane proteins, irradiated in the presence of Triton X-100, should be diminished by a factor of about 24% to obtain the value.
