Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.2.1.26 (
invertase
)
4,927
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
During refolding and reassociation of chemically denatured non-glycosylated
invertase
from Saccharomyces cerevisiae, aggregation competes with correct folding, leading to low yields of reactivation (
Kern
et al. (1992) Protein Sci. 1, 120-131). In the presence of the chaperone GroEL, refolding is completely arrested. This suggests the formation of a stable complex between GroEL and non-native non-glycosylated
invertase
. Addition of MgATP results in a slow release of active
invertase
from the chaperone complex. When GroEL/ES and MgATP are present during refolding, the final reactivation yield increases from 14% to 36%. In contrast, refolding of the core-glycosylated and the high-mannose glycosylated forms of
invertase
is not arrested by GroEL. Only a short lag phase at the beginning of reactivation and a slightly increased reactivation yield (64% to 86% for core-glycosylated and 62% to 76% for external
invertase
) indicate a weak interaction of the glycosylated forms with the chaperone.
...
PMID:Glycosylation inhibits the interaction of invertase with the chaperone GroEL. 136 29
