Effects of linoleic acid and cations on the activity of a novel high-molecular weight protease, ingensin, from human placenta.
A linoleic acid-sensitive protease, ingensin, was purified to homogeneity from human placenta. The physical properties of the placental ingensin were found to be very similar to those of skeletal muscle ingensin [Ishiura et al. (1985) FEBS Lett. 189, 119-123]. The purified ingensin was activated by linoleic acid and SDS. The linoleic acid-activated form was inhibited preferentially by divalent cations, whereas the SDS-activated form was inhibited by monovalent cations instead.
D002412:Cations; D003546:Cysteine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D005260:Female; D006801:Humans; D007700:Kinetics; D019787:Linoleic Acid; D008041:Linoleic Acids / Q000494:pharmacology*; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000302:isolation & purification / Q000378:metabolism*; D010920:Placenta / Q000201:enzymology*; D011247:Pregnancy; D046988:Proteasome Endopeptidase Complex
D002412:Cations; D008041:Linoleic Acids; D009097:Multienzyme Complexes; D019787:Linoleic Acid; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D046988:Proteasome Endopeptidase Complex