Linked Life Data

1280166

Source:http://linkedlifedata.com/resource/pubmed/id/1280166

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1992-12-30
pubmed:abstractText
Macro enzymes, i.e. complexes of normal (iso-)enzymes with an immunoglobulin, may be due to immunological cross-reactions evoked by specific viral antigenic determinants that are homologous to regions in the target enzymes. A search of the National Biomedical Research Foundation protein databank with the amino-acid sequence of human pancreatic amylase revealed a marked homology with a fragment of the yellow fever virus major envelope protein E: i.e. an overall identity of 19.7 per cent and a high degree (40.9 per cent) of conservative amino-acid substitutions over 119 amino acids. At each identical position, the corresponding residue of Taka amylase A was examined by three-dimensional structure analysis, to determine whether the position is likely to be buried or exposed. The existence of a site (epitope) on amylase recognized by an anti-amylase antibody is discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0939-4974
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
449-54
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Induction of autoantibodies to human enzymes following viral infection: a biologically relevant hypothesis.
pubmed:affiliation
Department of Clinical Chemistry, Onze Lieve Vrouwe Gasthuis, Amsterdam, The Netherlands.
pubmed:publicationType
Journal Article, Comparative Study