[Alkaline phosphatase in reverse micelles of surfactants in organic solvent].
A dimeric enzyme (alkaline phosphatase from calf intestinal mucosa) was studied in the reversed micellar medium of Aerosol OT (AOT) in octane. The dependence of the enzyme's activity on the hydration degree (on the size of micelles) is a curve with two optima corresponding to the hydration degrees [H2O]/[AOT] = 17 and 25; when the inner cavity radii of reversed micelles are equal to the size of the enzyme's monomer (Mr = 70 000) and of the dimer (Mr = 140 000). Ultracentrifugation experiments showed that a reversible dissociation of the enzyme into subunits takes place as a result of the change of the hydration degree; the first and second maxima corresponding to the functioning of the monomeric and dimeric forms of the enzyme, respectively.
Nametkin
S P
SP
Kabanov
A V
AV
Kliachko
N L
NL
Levashov
A B
AB
D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D002417:Cattle; D004143:Dioctyl Sulfosuccinic Acid; D007413:Intestinal Mucosa / Q000201:enzymology; D008823:Micelles; D011487:Protein Conformation; D013501:Surface-Active Agents; D014461:Ultracentrifugation
D008823:Micelles; D013501:Surface-Active Agents; D004143:Dioctyl Sulfosuccinic Acid; D000469:Alkaline Phosphatase
Shchelochnaia fosfataza v obrashchennykh mitsellakh PAV v organicheskom rastvoritele.