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Literature summary for 2.4.1.1 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
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Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
glycogen phosphorylase b
-
 Oryctolagus cuniculus
Phb
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 Oryctolagus cuniculus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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