Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C1389183 (autodigestion)
 317 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. A high-molecular-mass multicatalytic proteinase, ingensin, has been purified from rat liver and biochemically characterized. Trypsinization in the presence of ATP prevented the degradation of ingensin subunits. 2. Glutaraldehyde, which copolymerizes proteins, increased the apparent molecular mass of the subunits on SDS-PAGE, indicating the occurrence of covalent crosslinking of subunits. ATP, in this case, lowered the extent of covalent crosslinking. These results suggest that ATP altered the conformation of ingensin subunits. 3. Urea-induced autodigestion experiments demonstrated that some low-molecular-weight subunits selectively disappeared without changes in the contents of other subunits. The chymotryptic activity of the proteinase was more resistant to autodigestion than its tryptic activity. Therefore, we conclude that separate subunits of the enzyme are responsible for the different peptide-hydrolyzing activities.
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PMID:Molecular and biochemical properties of the ATP-stimulated multicatalytic proteinase, ingensin, from rat liver. 212 26