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Literature summary for 2.4.1.1 extracted from

  • Meremyanin, A.V.; Eronina, T.B.; Chebotareva, N.A.; Kleimenov, S.Y.; Yudin, I.K.; Muranov, K.O.; Ostrovsky, M.A.; Kurganov, B.I.
    Effect of alpha-crystallin on thermal aggregation of glycogen phosphorylase b from rabbit skeletal muscle (2007), Biochemistry (Moscow), 72, 518-528.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
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Oryctolagus cuniculus
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Synonyms

Synonyms Comment Organism
glycogen phosphorylase b
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Oryctolagus cuniculus
Phb
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Oryctolagus cuniculus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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the proposed scheme of thermal denaturation and aggregation of Phb includes the stage of reversible dissociation of dimers of Phb into monomers, the stage of the formation of the starting aggregates from the denatured monomers of Phb, and the stage of the sticking of the starting aggregates and higher order aggregates Oryctolagus cuniculus