Phosphorylation of zymogen granule membrane proteins in intact rat pancreatic acinar cells.
Phosphorylated substrates of molecular weights 130,000, 70,000, and 29,000, were identified by SDS-gel electrophoresis in zymogen granule membranes of rat pancreatic acinar cells incubated in vitro with protein kinase catalytic subunit. However, when intact cells were incubated with [32P]-orthophosphate, only the 29,000 molecular weight protein was phosphorylated.
D000818:Animals; D002384:Catalysis; D003594:Cytoplasmic Granules / Q000378:metabolism*; D004792:Enzyme Precursors / Q000378:metabolism*; D066298:In Vitro Techniques; D007425:Intracellular Membranes / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism*; D010179:Pancreas / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D012259:Ribonuclease, Pancreatic; D012270:Ribosomes / Q000378:metabolism
D004792:Enzyme Precursors; D008565:Membrane Proteins; D010750:Phosphoproteins; D011494:Protein Kinases; D012259:Ribonuclease, Pancreatic