3.4.17.12: carboxypeptidase M
This is an abbreviated version!
For detailed information about carboxypeptidase M, go to the full flat file.
Word Map on EC 3.4.17.12
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3.4.17.12
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pain
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women
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lymphocyte
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contralateral
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children
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postoperative
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prophylactic
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myelinolysis
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mastectomy
-
pontine
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knee
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cyclophosphamide
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unilateral
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wave
-
rehabilitation
-
hyponatremia
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decision
-
summation
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session
-
flexion
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accelerometer
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myoelectrical
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chlorpheniramine
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preoperative
-
arthroplasty
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noxious
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phytohemagglutinin
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3h-thymidine
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maleate
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pressor
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pain-free
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decision-making
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analgesia
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psychophysical
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actigraph
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pokeweed
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moderate-to-vigorous
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3h-tdr
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disomy
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myotomy
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cuff
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physiotherapy
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arthroscopic
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gastroparesis
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suprathreshold
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dysrhythmias
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breast-conserving
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medicine
-
trapezius
-
manometry
-
resting-state
-
diagnostics
- 3.4.17.12
- pain
- women
- lymphocyte
-
contralateral
- children
-
postoperative
-
prophylactic
- myelinolysis
-
mastectomy
- pontine
- knee
- cyclophosphamide
-
unilateral
-
wave
-
rehabilitation
- hyponatremia
-
decision
-
summation
-
session
-
flexion
-
accelerometer
-
myoelectrical
-
chlorpheniramine
-
preoperative
-
arthroplasty
-
noxious
- phytohemagglutinin
-
3h-thymidine
- maleate
-
pressor
-
pain-free
-
decision-making
-
analgesia
-
psychophysical
-
actigraph
-
pokeweed
-
moderate-to-vigorous
-
3h-tdr
-
disomy
-
myotomy
-
cuff
-
physiotherapy
-
arthroscopic
-
gastroparesis
-
suprathreshold
- dysrhythmias
-
breast-conserving
- medicine
-
trapezius
-
manometry
-
resting-state
- diagnostics
Reaction
cleavage of C-terminal arginine or lysine residues from polypeptides =
Synonyms
carboxypeptidase M, carboxypeptidase-M, CPM, M14006 (Merops-ID), More
ECTree
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Purification
Purification on EC 3.4.17.12 - carboxypeptidase M
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native enzyme from placental microvillus membranes by solubilization through either phosphatidylinositol-specific phospholipase C or CHAPS, ion exchange and arginine affinity chromatography, and gel filtration
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recombinant 3'-truncated, glycosylphosphatidylinositol-free, soluble enzyme from insect cells by anion exchange chromatography and gel filtration to homogeneity
recombinant enzyme 1753fold from Pichia pastoris strain GS115 by gel filtration and anion exchange chromatography to homogeneity
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recombinant proteins are purified by affinity chromatography, membrane extracts are prepared from rat lungs and loaded onto a heparin affinity column, followed by hydroxyapatite and cation exchange chromatographies
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the CPM secreted in the supernatant is purified by a two-step procedure consisting of gel filtration and ion-exchange chromatography
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wild type carboxypeptidase M, CPMwt, is purified from Pichia pastoris supernatant using hydrophobic interaction chromatography and affinity chromatography, hCPM is purified from human prostasomes