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Literature summary for 2.4.1.25 extracted from

  • Taylor, C.; Cox, A.J.; Kernohan, J.C.; Cohen, P.
    Debranching enzyme from rabbit skeletal muscle. Purification, properties and physiological role (1975), Eur. J. Biochem., 51, 105-115.
    View publication on PubMed
Search for more literature for 2.4.1.25

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
 1 * 120000, PAGE Oryctolagus cuniculus
155000
-
 sedimentation equilibrium Oryctolagus cuniculus
164000
-
 high-speed sedimentation equilibrium Oryctolagus cuniculus
166000
-
 SDS-PAGE Oryctolagus cuniculus
270000
-
 approach-to-equilibrium method Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
 rabbit
-

Purification (Commentary)

Purification (Comment) Organism
-
 Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
muscle skeletal muscle Oryctolagus cuniculus
-

Storage Stability

Storage Stability Organism
4°C, purified enzyme in buffer shows little or no loss of activity in 1 month Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 2 different enzyme activities, oligo-1,4-1,4-glucan-4-glycosyltransferase EC 2.4.1.25 and amylo-1,6-glucosidase EC 3.2.1.33 reside on the same polypeptide chain Oryctolagus cuniculus ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 166000, SDS-PAGE Oryctolagus cuniculus
monomer 1 * 120000, PAGE Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
oligo-1,4-1,4-glucantransferase
-
 Oryctolagus cuniculus