Akamizu T, Kosugi S, Kohn L D
Laboratory of Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892.
Biochem Biophys Res Commun. 1990 Jun 29;169(3):947-52. doi: 10.1016/0006-291x(90)91985-2.
In vitro transcription/translation, using rat thyrotropin receptor cDNA, results in the formation of nonglycosylated proteins able to bind thyrotropin, one of which approximates the 87 Kd size predicted for the receptor. In the presence of canine pancreatic microsomal membranes, putative glycosylation sites are modified as evidenced by digestion with endoglycosidase H. Using a deletion mutant, the presence of a hydrophobic peptide after the initiation signal is established as a signal peptide critical to post translational processing by the canine pancreatic membranes but not to binding thyrotropin.
使用大鼠促甲状腺激素受体互补脱氧核糖核酸进行体外转录/翻译，会形成能够结合促甲状腺激素的非糖基化蛋白，其中一种蛋白的大小接近预测的该受体的87千道尔顿。在犬胰腺微粒体膜存在的情况下，用内切糖苷酶H消化可证明推定的糖基化位点被修饰。使用缺失突变体，起始信号后疏水肽的存在被确定为对犬胰腺膜的翻译后加工至关重要但对结合促甲状腺激素不重要的信号肽。
