[Artificial oligomerization of enzymes--a new way of regulating their catalytic activity in reversed micellar systems]. / Iskusstvennaia oligomerizatsiia fermentov--novyi put' k regululiatsii ikh kataliticheskoi aktivnosti v sistemakh obrashchennykh mitsell.
Bioorg Khim
; 17(6): 756-9, 1991 Jun.
Article
en Ru
| MEDLINE
| ID: mdl-1723269
ABSTRACT
Comparative studies were carried out in the catalytic activity regulation of native alpha-chymotrypsin and its artificially produced hexameric form as an example of non-dissociating oligomeric enzyme (covalently cross-linked by means of succinimidyl-3-(2-pyridylthiopropionate] in the Aerosol OT reversed micelles in octane. Native (monomeric) alpha-chymotrypsin exhibits maximal catalytic activity in the reversed micelles at the hydration degree w0 = 10, when the radius of the micelle inner cavity is equal to the radius of the alpha-chymotrypsin globule. For the alpha-chymotrypsin hexamer, optimum is observed at w0 = 45, with the inner micellar cavity radius (r = 68 A) being approximately equal to the radius of the sphere surrounding the octahedral combination of the six monomeric alpha-chymotrypsin molecules (r = 61 A). Thus, construction of the corresponding oligomeric structures is made easy, with the optimal catalytic activity in a preset range of the hydration degrees.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Quimotripsina
/
Micelas
Límite:
Animals
Idioma:
Ru
Revista:
Bioorg Khim
Año:
1991
Tipo del documento:
Article