Rubinstein M, Stein S, Udenfriend S
Proc Natl Acad Sci U S A. 1978 Feb;75(2):669-71. doi: 10.1073/pnas.75.2.669.
The high molecular weight (approximately 30,000) precursor to opioid activity (pro-opiocortin) previously detected in extracts of rat pituitary was digested with trypsin and the resulting peptide mixture was resolved by high-performance reverse-phase chromatography. A peak of opioid activity was eluted at the position of the nonapeptide beta-LPH (61-69), which was also the same fragment obtained by trypsin digestion of betas-lipotropin or beta-endorphin. This identified the protein as a precursor to the endorphins and Met-enkephalin. No activity was detected in the position corresponding to the Leu5 analog of betas-LPH (61-69), thus ruling out the possibility of a beta-lipotropin-like precursor to Leu-enkephalin in pituitary extracts. Pro-opiocortin and beta-lipotropin are present in rat pituitary extracts in comparable amounts, approximately 10 pmol/mg of tissue.
先前在大鼠垂体提取物中检测到的阿片样物质活性高分子量(约30,000)前体(阿片促皮质素原)用胰蛋白酶消化,所得肽混合物通过高效反相色谱法分离。阿片样物质活性峰在九肽β-LPH(61-69)的位置洗脱,这也是通过对β-促脂素或β-内啡肽进行胰蛋白酶消化获得的相同片段。这确定该蛋白质为内啡肽和甲硫氨酸脑啡肽的前体。在与β-LPH(61-69)的亮氨酸5类似物相对应的位置未检测到活性,从而排除了垂体提取物中存在亮氨酸脑啡肽的β-促脂素样前体的可能性。阿片促皮质素原和β-促脂素以相当的量存在于大鼠垂体提取物中,约为10 pmol/mg组织。