AMP deaminase in the gill of trout (Salmo gairdneri R.). Modalities of an activation by cellular proteolytic enzymes.
1. The AMP deaminase activity present in a crude extract of trout gill increased with time. 2. Soybean trypsin inhibitor and alpha2-macroglobulin inhibited the AMP deaminase activation. NEM was also inhibitory at 10-3 M. 3. The activation process is followed by a decrease of activity which is inhibited by EGTA and enhanced by Mg2+. These two compounds were without effect on the activation process itself. 4. Trypsin induces a sharp activation of AMP deaminase in a fresh gill extract but is without effect on a fully activated extract. 5. Overall, the results suggest that neutral proteinases are implicated in AMP deaminase activation.
D000659:AMP Deaminase / Q000378:metabolism*; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D004533:Egtazic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D005880:Gills / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008274:Magnesium / Q000494:pharmacology; D009709:Nucleotide Deaminases / Q000378:metabolism*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000494:pharmacology; D011685:Purine Nucleotides / Q000032:analysis; D012487:Salmonidae / Q000378:metabolism*; D013439:Sulfhydryl Reagents / Q000494:pharmacology; D013997:Time Factors; D014337:Trout / Q000378:metabolism*; D014357:Trypsin / Q000378:metabolism; D000511:alpha-Macroglobulins / Q000378:metabolism
D011480:Protease Inhibitors; D011685:Purine Nucleotides; D013439:Sulfhydryl Reagents; D000511:alpha-Macroglobulins; D004533:Egtazic Acid; D010447:Peptide Hydrolases; D014357:Trypsin; D009709:Nucleotide Deaminases; D000659:AMP Deaminase; D008274:Magnesium