In:
Journal of Molecular Recognition, Wiley, Vol. 17, No. 5 ( 2004-09), p. 426-432
Abstract:
Self‐association of phosphorylase kinase (PhK) and its interaction with glycogen ( M =5500 kDa) and phosphorylase b (Ph b ) has been studied using analytical ultracentrifugation and turbidimetry under the conditions of molecular crowding arising from the presence of high concentrations of osmolytes. In accordance with the predictions of the molecular crowding theory, trimethylamine N ‐oxide (TMAO) and betaine greatly favor self‐association of PhK induced by Mg 2+ and Ca 2+ and PhK interaction with glycogen. In contrast, proline suppresses these processes, probably, due to its specific interaction with PhK. All osmolytes tested prevented the complex formation between PhK and its physiological substrate, Ph b . The specific interactions of PhK and Ph b with glycogen, in the living cell, presumably is a factor allowing the negative effect of crowding on the recognition of Ph b by PhK to be overcome. Copyright © 2004 John Wiley & Sons, Ltd.
Type of Medium:
Online Resource
ISSN:
0952-3499
,
1099-1352
Language:
English
Publisher:
Wiley
Publication Date:
2004
detail.hit.zdb_id:
1491198-X
SSG:
12
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