Heat induced aggregation of the sodium dodecyl sulfate-solubilized main intrinsic polypeptide isolated from bovine lens plasma membrane.
Heat induced aggregation of the sodium dodecyl sulfate-solubilized main intrinsic polypeptide isolated from bovine lens plasma membrane.
复制标题
从牛晶状体质膜分离的十二烷基硫酸钠溶解的主要内在多肽的热诱导聚集。
DOI：
10.1016/0006-291x(78)90277-2
复制
发表时间：
1978
影响因子：
3.1
通讯作者：
J. Horwitz
中科院分区：
文献类型：
--
作者：
M. M. Wong;N. Robertson;J. Horwitz
One major component of lens plasma membrane is a glycoprotein that SDS-polyacrylamide gel electrophoresis shows to possess an apparent molecular weight of 26,000. When this protein is solubilized in low ionic strength buffers containing SDS, and heated to 100° for 1 to 3 min prior to electrophoresis, conversion into high molecular weight aggregate results. The heat lability of this protein is greatly enhanced if it solubilized and heated in buffers containing 0.1 M NaCl. At this ionic strength, incubation for 3 h at 38° results in conversion of 20% of the protein into high melecular weight aggregates. Most other membrane proteins isolated from lens membrane are insensitive to heat treatment. It is concluded that temperature and ionic strength must be recorded and controlled carefully when using SDS-polyacrylamide gel electrophoresis to study this membrane protein.
