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

  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},
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.
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
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.
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.
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
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


Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acids or sodium dodecyl sulphate.
In contrast with the non-activated proteinase, the activated enzyme considerably degrades muscle cytoplasmic proteins in vitro, so it is not unlikely that, in vivo, potential activators such as fatty acids can induce the multicatalytic proteinase to participate in muscle protein breakdown. Expand
Purification and characterization of a multicatalytic high-molecular-mass proteinase from rat skeletal muscle.
A proteolytic enzyme was purified from the post-myofibrillar fraction of rat skeletal muscle and appeared to be homogeneous as judged by disc electrophoresis in polyacrylamide gels and by immunoelectrophoresIS. Expand
Preferential degradation of the oxidatively modified form of glutamine synthetase by intracellular mammalian proteases.
  • A. Rivett
  • Medicine, Biology
  • The Journal of biological chemistry
  • 1985
Four intracellular proteases partially purified from liver preferentially degraded the oxidatively modified (catalytically inactive) form of glutamine synthetase, suggesting that oxidative modification may be involved in intrACEllular protein turnover. Expand
Canine cardiac calcium‐dependent proteases: Resolution of two forms with different requirements for calcium
Two Ca2+dependent protease activities from canine cardiac extracts were separated and partially purified and one of the forms was found to be active at free-Ca2+ concentrations which may be attained in muscle cells during contraction. Expand
Minireview: Calcium-dependent proteolysis in living cells
Calcium ion, one of the second messengers in living organisms, has various functions including the ability to enhance intracellular proteolysis, which occurs in the cytosol or membrane rather than in the lysosome. Expand
Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates.
Homogeneous porcine calpain (Ca2+-dependent cysteine proteinase) was found to hydrolyze a variety of peptides and synthetic substrates and the specificity and kinetics of calpains I and II were described. Expand
Autolysis of calcium-activated neutral protease of chicken skeletal muscle.
MuCANP is produced from mCANP only by the specific autolysis of mCANp, and muCANP did not yield muCAN p from m CANP at lower Ca2+ concentrations where only muCANp was active. Expand
Proteolytic activation of calcium-activated, phospholipid-dependent protein kinase by calcium-dependent neutral protease.
It is noted that Ca2+ protease II, which is active at higher concentrations of Ca2+, proteolytically activates protein kinase C irrespective of the presence and absence of phospholipid and diacylglycerol. Expand
Biochemistry 7, 2116-2122
  • FEBS Lett. 109,
  • 1968