Linked Life Data

8651692

Source:http://linkedlifedata.com/resource/pubmed/id/8651692

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1996-7-22
pubmed:abstractText
Acid-induced and guanidine hydrochloride (GdnCl)-induced reversible unfolding of Escherichia coli alkaline phosphatase (AP) was characterized under equilibrium conditions. The protein was exposed to extreme conditions of pH 2.0 or 6 M GdnCl and was subsequently returned to normal conditions. Associated changes in the protein structure was probed by various spectroscopic methods. The changes in the functional properties were monitored by measuring enzymatic activity, capacity to renature spontaneously upon removal of the denaturant, and renaturation in presence of various site-specific and nonspecific effector molecules, in the absence and presence of beta-mercaptoethanol. Analysis of the fluorescence and CD spectra showed that the unfolding of the organized structures was much more extensive in 6 M GdnCl than at pH 2.0. Intrachain S-S bonds in each unfolded state were accessible to reduction by beta-mercaptoethanol. The effectors Zn2+ and ATP induced renaturation of active site only under reducing conditions, whereas Triton X-100 or alpha-crystallin needed the presence of some organized structure. The reconstituted protein from each denatured state without or with an effector showed different CD spectra. It is concluded that the active site domain of AP could be reconstituted independently of other structural domains in different pathways.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
330
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
174-80
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Reversible unfolding of Escherichia coli alkaline phosphatase: active site can be reconstituted by a number of pathways.
pubmed:affiliation
Department of Biochemistry and Biophysics, University of Kalyani, India.
pubmed:publicationType
Journal Article