Isolation of two forms of the high‐molecular‐mass serine protease, ingensin, from porcine skeletal muscle

@article{Ishiura1985IsolationOT,
  title={Isolation of two forms of the high‐molecular‐mass serine protease, ingensin, from porcine skeletal muscle},
  author={S. Ishiura and M. Sano and K. Kamakura and H. Sugita},
  journal={FEBS Letters},
  year={1985},
  volume={189}
}
Porcine muscle Protease SDS‐activation 
Addition of ATP increases the apparent molecular mass of the multicatalytic proteinase, ingensin
Multicatalytic proteinase; Isoenzyme; ATP; (Rat liver)
Action of a serine proteinase from fish skeletal muscle on myofibrils.
TLDR
The action of a serine proteinase from fish skeletal muscle on myofibrils was studied and it was found that proteolysis could be completely prevented by the addition of a trypsin inhibitor isolated from the same muscle. Expand
Localization of ingensin in rat central nervous system and skeletal muscle
TLDR
A high molecular weight, fatty acid‐ and SDS‐sensitive protease named ingensin was purified from rat brain in this study and Immunoblot bands were detected in the same positions as those in the case of ingensIn from rat liver. Expand
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 skeletalExpand
Activity measurement of lysosomal cysteine proteinases, cathepsins B, H and L, in crude tissue extracts, and their relation to the fractional rate of protein degradation
Abstract 1. 1. The fractional rate of protein degradation was measured in vivo and compared with the lysosomal enzyme activities of several rat tissues. Good agreement was observed between them. 2.Expand
Human erythrocyte multicatalytic proteinase: activation and binding to sulfated galacto- and lactosylceramides.
Chymotrypsin-like activity of multicatalytic proteinase (MCP) purified from human erythrocytes was selectively activated 2.5--3.5-fold by sulfated glycolipids such as galactosylceramide sulfate (SM4)Expand
Molecular and biochemical properties of the ATP-stimulated multicatalytic proteinase, ingensin, from rat liver.
TLDR
It is concluded that separate subunits of the enzyme are responsible for the different peptide-hydrolyzing activities of ingensin, and ATP lowered the extent of covalent crosslinking of subunits. Expand
Ingensin, a fatty acid-activated serine proteinase from rat liver cytosol.
TLDR
The addition of glycerol and nordihydroguaiaretic acid lowered the extent of its activation by fatty acids as well as its intrinsic peptide-hydrolyzing activity, suggesting that the enzyme is a serine proteinase with an active thiol group(s) near the active site. Expand
Induction of carp muscle multicatalytic proteinase activities by sodium dodecyl sulfate and heating
Abstract 1. 1. A multicatalytic proteinase (MCP) was purified from carp muscle by chromatography of DEAE-cellulose, hydroxylapatite and AcA34 to homogeneous. 2. 2. This MCP had three distinctExpand
The multicatalytic proteinase of mammalian cells
TLDR
Inhibition of proteinase activity by thiol reagents supports the suggestion that the enzyme is a cysteineproteinase but there is some evidence that it may be a serine proteinase and the catalytic mechanism is at present unknown. Expand
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