Linked Life Data

10543984

Source:http://linkedlifedata.com/resource/pubmed/id/10543984

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-12-22
pubmed:abstractText
Ervatamin C, a novel cysteine protease, belongs to alpha + beta class of proteins, probably with two domains, and retains both secondary and tertiary structures along with biological activity over a wide range of pH (2-12). Under neutral conditions, GuHCl and temperature-induced unfolding was cooperative with high transition midpoints and shows no structural changes in the presence of urea reflecting a remarkable stability. The fluorescence emission maximum at 350 nm suffers a blue shift of 4-5 nm upon lowering the pH and a red shift of 5 nm under denatured conditions. Unfolding transition curves at pH 2.0 are non-coincidental indicating the presence of intermediates in the unfolding pathway. At extremely low pH, the enzyme loses all the tertiary structure and proteolytic activity but retains a predominant secondary structure and a strong binding to ANS. GuHCl-induced unfolding of the enzyme in this intermediate state is noncooperative and indicates sequential unfolding of the domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
635-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Structural characterization of a highly stable cysteine protease ervatamin C.
pubmed:affiliation
Molecular Biology Unit, Institute of Medical Sciences, Banaras Hindu University, Varanasi, 221 005, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't