Abstract
To learn more about the subcellular localization and nature of the enzymes involved in the post-translational processing of pro-ACTH/endorphin, separated rat anterior and intermediate pituitary tissue was homogenized and fractionated into subcellular organelles. Use of Percoll as a centrifugation material resulted in an excellent purification of secretory granules from pituitary tissue in a short period of time with very little handling. The purity of the granule and rough endoplasmic reticulum fractions was assessed by electron microscopy and by assays of marker enzymes for mitochondria (fumarase), rough endoplasmic reticulum (NADPH-cytochrome C reductase), Golgi (galactosyl transferase), and cytoplasm (lactate dehydrogenase). The amount of each form of ACTH and β-endorphin in the granule fraction, the rough endoplasmic reticulum/Golgi fraction and homogenate was determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis and radioimmunoassay. In both lobes of the pituitary the granule fractions were relatively enriched in the smaller peptide products derived from pro-ACTH/endorphin, while the rough endoplasmic reticulum/Golgi fractions were enriched in common precursor.
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