Linked Life Data

2484938

Source:http://linkedlifedata.com/resource/pubmed/id/2484938

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-5-6
pubmed:abstractText
A causal relationship between the presence of sialic acid and erythrocyte sialoglycoprotein-specific silver staining (Dzandu et al. 1984) has been examined. Quantitative chemical hydrolysis of sialic acid resulted in total loss of sialoglycoprotein-specific staining suggesting a causal role for sialic acid. It is speculated that under acidic conditions, the highly nucleophilic carboxylates of sialic acid (pKa = 2.6), may determine staining specificity by functioning as primary silver-reactive centers. Because selective staining was abrogated on gel treatment with aldehydes, alkali, thiol reagents or by temperature elevation, it is inferred that the above physico-chemical variables nullified selective staining by creating additional silver nucleation sites which culminate in non-specific staining. Acid treatment of ghosts at 80 degrees C, a standard method for sialic acid hydrolysis caused very specific polypeptide scissions, presumably at aspartyl-proline bonds. Because of the high reproducibility of the membrane protein fragmentation patterns, this method should be ideal for rapid peptide mapping of complex protein mixtures without recourse to isolating and purifying the individual polypeptides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0954-6642
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
137-44
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Role of sialic acid in selective silver staining of red cell glycophorins.
pubmed:affiliation
Department of Anatomy and Cell Biology, Texas College of Osteopathic Medicine, Fort Worth 76107.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't