与内质网腔相关的肽基脯氨酰顺反异构酶活性。
Peptidyl prolyl cis-trans-isomerase activity associated with the lumen of the endoplasmic reticulum.
作者信息
Bose S, Freedman R B
机构信息
Research School of Biosciences, Biological Laboratory, University of Kent, Canterbury, U.K.
出版信息
Biochem J. 1994 Jun 15;300 ( Pt 3)(Pt 3):865-70. doi: 10.1042/bj3000865.
Abstract
Peptidyl prolyl cis-trans-isomerase (PPI) activity was detected in microsomal fractions from bovine and rat liver. Extensive washing, proteinase and sonication treatments indicated that although some of this activity was due to adsorbed cytosolic enzymes, there was also an active but latent microsomal PPI activity. Density-gradient subfractionation indicated that activity was associated with vesicles derived from both the rough and the smooth endoplasmic reticulum (ER), suggesting that the activity was located within the ER lumen. The luminal PPI activity was inhibited by cyclosporin A and was active towards an unfolded protein substrate as well as towards the standard peptide substrate.
摘要
在牛和大鼠肝脏的微粒体部分检测到肽基脯氨酰顺反异构酶（PPI）活性。大量洗涤、蛋白酶处理和超声处理表明，虽然部分活性归因于吸附的胞质酶，但也存在一种活跃但潜伏的微粒体PPI活性。密度梯度亚分级分离表明，该活性与来自粗面和滑面内质网（ER）的囊泡相关，这表明该活性位于内质网腔中。腔内PPI活性受环孢菌素A抑制，并且对未折叠的蛋白质底物以及标准肽底物均有活性。
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