3.4.22.52: calpain-1
This is an abbreviated version!
For detailed information about calpain-1, go to the full flat file.
Word Map on EC 3.4.22.52
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3.4.22.52
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calpains
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calpastatin
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ca2+-dependent
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tender
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calcium-dependent
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meat
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cytoskeletal
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beef
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ischemia
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myofibrillar
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hippocampal
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calpeptin
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autolysis
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caspase
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proteinase
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spectrin
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longissimus
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calpain-mediated
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postmortem
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cathepsins
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calpain-specific
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leupeptin
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lumborum
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medicine
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sarcomere
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non-lysosomal
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nebulin
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calpain-dependent
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slaughter
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calpain-like
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semimembranosus
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fodrin
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food industry
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carcass
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angus
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autoproteolysis
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warner-bratzler
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autolyzed
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ca2+-activated
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steak
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caspase-12
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myofibril
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talin
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troponin-t
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brahman
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calmodulin-like
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thoracis
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proteolyzed
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aif
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canps
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alpha-spectrin
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desmin
- 3.4.22.52
- calpains
- calpastatin
-
ca2+-dependent
-
tender
-
calcium-dependent
-
meat
- cytoskeletal
- beef
- ischemia
- myofibrillar
- hippocampal
- calpeptin
-
autolysis
-
caspase
- proteinase
- spectrin
- longissimus
-
calpain-mediated
-
postmortem
- cathepsins
-
calpain-specific
- leupeptin
- lumborum
- medicine
-
sarcomere
-
non-lysosomal
-
nebulin
-
calpain-dependent
-
slaughter
-
calpain-like
- semimembranosus
- fodrin
- food industry
-
carcass
-
angus
-
autoproteolysis
-
warner-bratzler
-
autolyzed
-
ca2+-activated
-
steak
- caspase-12
- myofibril
- talin
-
troponin-t
-
brahman
-
calmodulin-like
- thoracis
-
proteolyzed
- aif
-
canps
- alpha-spectrin
- desmin
Reaction
broad endopeptidase specificity =
Synonyms
Cal 1, calcium-activated neutral protease I, calpain 1, calpain 1-gamma, calpain 1A, calpain I, calpain small subunit, calpain-1, calpain-1 (micro-form), calpain-I, calpain1, CANP1, CAPN1, CAPN1 g.p. (Homo sapiens), CAPN2, CAPNS1, cysteine protease, EC 3.4.22.17, EC 3.4.24.5, m-CANP, micro-calpain, mit-CPN1, mito-mu-calpain, mu-calpain, muCANP, muI-II
ECTree
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General Stability
General Stability on EC 3.4.22.52 - calpain-1
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m-calpain loses 50-55% of its proteolytic activity within 5 min during incubation at pH 7.5 in 300 mM or high salt and at a slower rat in 100 mM salt. This loss of activity is not reversed by dialysis for 18 h against a low-ionic-strength buffer at pH 7.5. Proteolytic activity of the unautolyzed calpains is not affected by incubation for 45 min at ionic strength up to 1000 mM. Ionic strengths of 100 mM or above cause dissociation of the two subunits of autolyzed calpains. The dissociated large subunits aggregate to form dimers and trimers, which are proteolytically inactive
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