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Literature summary extracted from

  • Meremyanin, A.V.; Eronina, T.B.; Chebotareva, N.A.; Kurganov, B.I.
    Kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle: mechanism of protective action of alpha-crystallin (2008), Biopolymers, 89, 124-134.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Oryctolagus cuniculus
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-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.4.1.1 skeletal muscle
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 Oryctolagus cuniculus
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.1 glycogen + glucose 1-phosphate
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 Oryctolagus cuniculus glycogen + phosphate
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 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.1 glycogen phosphorylase b
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 Oryctolagus cuniculus
2.4.1.1 Phb
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 Oryctolagus cuniculus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.4.1.1 48
-
 kinetics of thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle is studied by dynamic light scattering. The aggregation process proceeds in the regime of diffusion-limited cluster-cluster aggregation. In the presence of alpha-crystallin, a protein possessing the chaperone-like activity, the process of protein aggregation switches to the regime of reactionlimited cluster–cluster aggregation. The addition of alpha-crystallin raises the rate of thermal inactivation of Phb Oryctolagus cuniculus