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Literature summary for 2.7.3.2 extracted from

  • Pancera, S.M.; Gliemann, H.; Schimmel, T.; Petri, D.F.
    Effect of pH on the adsorption and activity of creatine phosphokinase (2006), J. Phys. Chem. B, 110, 2674-2680.
    View publication on PubMed
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Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus P00563 commercial preparation
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Source Tissue

Source Tissue Comment Organism Textmining
muscle
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 Oryctolagus cuniculus
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Subunits

Subunits Comment Organism
More study on adsorption of creatine kinase onto silicon wafers. At pH 4, enzyme monomers in solution adsorb, forming a very thin layer indicating creatine kinase unfolding. At pH 6.8, the adsorbed layer is composed of a mixture of enzyme dimers in native structure and film thickness is increased. At pH 9, creatine kinase dimers form monolayers with the higest thickness. In comparison to free enzyme in solution, adsorbed enzyme presents a shift of the optimal pH value from 6.8 toward alkaline pH Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
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 in comparison to free enzyme in solution, enzyme adsorbed onto silicon wafers presents a shift of the optimal pH value toward alkaline pH Oryctolagus cuniculus
6.8
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 native enzyme in solution Oryctolagus cuniculus