Linked Life Data

6544680

Source:http://linkedlifedata.com/resource/pubmed/id/6544680

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-1-23
pubmed:abstractText
Tetrameric lactate dehydrogenase from Bacillus stearothermophilus exhibits unusual stability towards high hydrostatic pressure: In contrast to the mesophilic enzyme, incubation at pressures up to 2.8 kbar does not cause irreversible denaturation. Hybridization under these conditions suggests partial dissociation to the dimer, indicating that reassociation occurs within the dead-time after pressure release (less than 20 s at less than or equal to 40 micrograms/ml, 20 degrees C). Incubation at P less than 2.8 kbar affects neither the native quaternary structure nor the catalytic function of the enzyme. Reconstitution of the unfolded and dissociated subunits after denaturation, e.g., in 6 M guanidine . HC1, is characterized by fast association favouring the native assembled structure. Evidence from spectroscopic measurements shows that reconstitution starts with a fast refolding reaction generating a native-like conformation. The subsequent rate-determining transconformation of the "structured monomers" governs the kinetics of reactivation and reassociation as one single first-order process. Chemical crosslinking with glutaraldehyde proves that the "structured monomers" undergo fast association to form the tetrameric final state of reconstitution, with significant amounts of dimeric intermediates being detectable. The renatured enzyme is indistinguishable from the native enzyme regarding its physicochemical and enzymological properties (e.g., activation by fructose-1,6-bisphosphate, and susceptibility towards proteolytic digestion).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0175-7571
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
87-94
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
High pressure dissociation of lactate dehydrogenase from Bacillus stearothermophilus and reconstitution of the enzyme after denaturation in 6 M guanidine hydrochloride.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't