Roth K A, Unanue R A, Leykam J, Tyler A N
Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.
Regul Pept. 1987 Dec;19(5-6):335-44. doi: 10.1016/0167-0115(87)90175-3.
Using a radioimmunoassay specific for the carboxyl terminus of beta-endorphin-(1-9) large amounts of beta-endorphin-(1-9)-immunoreactive material was detected in the human pituitary. The major peak of immunoreactivity was purified and characterized by fast atom bombardment-mass spectrometry and Edman degradation sequencing as authentic beta-endorphin-(1-9). In the rat pituitary the highest concentration of beta-endorphin-(1-9) immunoreactivity was in the posterior neurointermediate lobe. This material was identified as N-acetyl beta-endorphin-(1-9) by multiple radioimmunoassays, gel chromatography, and reversed-phase high-performance liquid chromatography. Control experiments determined that beta-endorphin-(1-9) was not formed postmortem or during the extraction procedure. These studies suggest that single lysine residues, similar to single arginine residues, are potential sites of posttranslational processing.
使用针对β-内啡肽-（1-9）羧基末端的放射免疫分析法，在人垂体中检测到大量β-内啡肽-（1-9）免疫反应性物质。免疫反应性的主要峰通过快原子轰击质谱法和埃德曼降解测序进行纯化和表征，确认为真实的β-内啡肽-（1-9）。在大鼠垂体中，β-内啡肽-（1-9）免疫反应性的最高浓度位于神经中间叶后部。通过多种放射免疫分析法、凝胶色谱法和反相高效液相色谱法，该物质被鉴定为N-乙酰基β-内啡肽-（1-9）。对照实验确定β-内啡肽-（1-9）不是在死后或提取过程中形成的。这些研究表明，与单个精氨酸残基类似，单个赖氨酸残基是翻译后加工的潜在位点。
