Arginine esterase from isolated dog prostate secretory granules is fully active enzymatically.
We have isolated secretory granules from dog prostate homogenates and have determined whether a major portion of arginine esterase was localized in this fraction and if it was enzymatically active. Secretory granules were purified by density gradient centrifugation on sucrose, metrizamide, or Percoll. A major proportion of whole prostate homogenate arginine esterase was found in the granule fractions. Furthermore, the specific enzymatic activity in the granules was similar to the one observed in seminal plasma. No evidence could be found for the existence of significant amount of a zymogen inactive form of arginine esterase. These results suggest that arginine esterase could be active within the secretory granules in vivo and that it could hydrolyze protein substrates contained in this organelle.
D000135:Acid Phosphatase / Q000378:metabolism; D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D003594:Cytoplasmic Granules / Q000201:enzymology*; D004285:Dogs; D066298:In Vitro Techniques; D008297:Male; D008854:Microscopy, Electron; D011467:Prostate / Q000201:enzymology* / Q000648:ultrastructure; D011506:Proteins / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology
D011506:Proteins; C019724:arginine esterase; D002265:Carboxylic Ester Hydrolases; D000135:Acid Phosphatase