Literature summary for 2.7.3.2 extracted from

Zou, H.; Yu, Z.; Wang, Y.; Yang, J.; Zhou, H.; Meng, F.; Park, Y.
Monomeric creatine kinase aggregation and sodium dodecyl sulfate-cyclodextrin assisted refolding (2007), J. Biomol. Struct. Dyn., 24, 359-367.

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
study on enzyme aggregation and reassociation in presence of sodium dodecyl sulfate-cyclodextrin. Aggregation does not occur at concentrations below 0.002 mM or temperature below 17°C. Trapping of monomeric creatine kinase variants such as thiol residue modified enzyme, sodium dodecyl sulfate binding enzyme, cyclodextrin treated enzyme, or dithiothreitol treated enzyme. Reassociation in presence of sodium dodecly sulfate-cyclodextrin follows first-order kinetics	Oryctolagus cuniculus

Renatured (Comment)

Organism

study on enzyme aggregation and reassociation in presence of sodium dodecyl sulfate-cyclodextrin. Aggregation does not occur at concentrations below 0.002 mM or temperature below 17°C. Trapping of monomeric creatine kinase variants such as thiol residue modified enzyme, sodium dodecyl sulfate binding enzyme, cyclodextrin treated enzyme, or dithiothreitol treated enzyme. Reassociation in presence of sodium dodecly sulfate-cyclodextrin follows first-order kinetics

Oryctolagus cuniculus

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	-	Oryctolagus cuniculus	-

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Release 2023.1 (January 2023)