Processing of the Common Precursor to ACTH and Endorphin in Mouse Pituitary Tumor Cells and Monolayer Cultures from Mouse Anterior Pituitary

摘要: Adrenocorticotropin (ACTH) and β-lipotropin (β-LPH) have been shown to be derived from the same high-molecular-weight precursor protein (common precursor) in mouse pituitary tumor cells (AtT-20/D16v cells) (Mains et al., 1977; Nakanishi Roberts Herbert, 1977a, b). When messenger RNA AtT-20 is translated a reticulocyte cell-free system, single form of synthesized with molecular weight 28,500 (28.5K pro-ACTH-endorphin) (Roberts 1977a,b). The use “polysome runoff technique” (Dintzis, 1961) has made it possible arrange tryptic peptides ACTH β-LPH relative one another 1977b) 28.5K as model structure Fig. 1. In this model, located at C terminus adjacent near middle molecule, leaving an unidentified sequence approximately 100 amino acids N terminus. A 31,000-molecular-weight isolated very similar that depicted 1 (Eipper Mains, 1978). Thus, contains α(l–39)ACTH, α-melanocyte-stimulating hormone (α-MSH), component hormones β-LPH: β-endorphin, β-MSH, Met-enkephalin.