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Literature summary for 3.1.1.8 extracted from

  • Alsen, C.; Bertram, U.; Gersteuer, T.; Ohnesorge, F.K.
    Studies on acetylcholinesterase and cholinesterase covalently bound to polymaleinic anhydride (1975), Biochim. Biophys. Acta, 377, 297-302.
    View publication on PubMed

Application

Application Comment Organism
analysis covalent coupling of the enzyme to a copolymerisate of maleinic anhydride and butanedioldivinylether provides the possibility to yield stable enzyme preparations Equus caballus

Organism

Organism UniProt Comment Textmining
Equus caballus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
serum
-
Equus caballus
-

Storage Stability

Storage Stability Organism
4°C, 140 days, stock solution, 75% loss of initial activity Equus caballus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
butyrylcholine + H2O
-
Equus caballus butanoate + choline
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
45
-
bound enzyme Equus caballus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
10 min, 10% loss of activity Equus caballus
60
-
10 min, 70% loss of activity Equus caballus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2 8.7 bound enzyme, no definite optimum, butyrylcholine Equus caballus