Linked Life Data

18214981

Source:http://linkedlifedata.com/resource/pubmed/id/18214981

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-6-3
pubmed:abstractText
Asparaginyl deamidation is a common form of nonenzymatic degradation of proteins and peptides. As it introduces a negative charge spontaneously and irreversibly, charge heterogeneity can be accumulated in protein solution during purification, preservation, and experiments. In this study, canine milk lysozyme (CML), a useful model for the study of the molten globule state, exhibited charge heterogeneity after sample purification. Four Asn residues in CML deamidated rapidly under mild conditions: pH 8.0 and 30 degrees C. Other than these residues, one Asn residue, which was stable in the native state, was labile to deamidation in the unfolded state. This suggests that the structural formation around Asn can suppress deamidation. Substitutions of these labile Asn residues to Gln residues prevented deamidation effectively. Because the substitutions did not disrupt the structural formation of the native and molten globule states, they will enable more precise analyses for physical and structural studies.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1097-0134
pubmed:author
pubmed:copyrightInfo
2008 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:volume
72
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
313-22
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Spontaneous asparaginyl deamidation of canine milk lysozyme under mild conditions.
pubmed:affiliation
Graduate School of Science, Hokkaido University, Sapporo, Hokkaido, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't