Linked Life Data

1270440

Source:http://linkedlifedata.com/resource/pubmed/id/1270440

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1976-8-3
pubmed:abstractText
Studies on the mechanism of the glutathione regeneration (Saxena, V.P., and Wetlaufer, D.B. (1970) Biochemistry 9, 5015-5023) of hen egg lysozyme have been carried out. The first two stoichiometric disulfides in lysozyme are formed about 8 times more rapidly than the second two. Almost no enzymic activity is regained until the first two disulfides are formed, thus ruling out an all-or-none mechanism. The disulfide peptides formed early in the regeneration have been isolated and identified. The results show a limited search of folding intermediates, and outline a folding pathway. The early disulfides involve cysteinyl residues III, IV, V, and VI. At the same time cysteinyl residues I, II, VII, and VIII are still reduced, as demonstrated by their isolation as S-alkylated derivatives. At slightly later times a peptide is found which contains the (native) disulfide between cysteinyl residues II and VII. It is likely, but as yet unproven, that formation of disulfide I-VIII completes the cross-linking of lysozyme.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
251
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3147-53
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
The folding pathway of reduced lysozyme.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.