Linked Life Data

9137643

Source:http://linkedlifedata.com/resource/pubmed/id/9137643

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-5-13
pubmed:abstractText
The structure of the Ascaris allergen, ABA-1 was characterized at several levels. Purified allergen monomers eluted from reducing PAGE were found to reassociate into dimers in phosphate buffered saline containing 0.9 mM Ca2+. This association may involve the formation of disulfide bonds between monomers. The primary amino acid sequence was used to predict secondary structure and compare the allergen to other known proteins sequences. ABA-1 appears to be highly helical protein of two domains. Sequence analysis reveals short regions (25 amino acids) of high homology (76%) between ABA-1 and the major body wall myosin of Onchocerca volvulus. In addition, ABA-1 has sequence similarity to a family of EF-hand containing calcium binding proteins called S100 proteins. The dimerization and two-domain structure of ABA-1 is consistent with the possibility that ABA-1 is a member of the S100 family of calcium binding proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1252-607X
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
41-8
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9137643-Allergens, pubmed-meshheading:9137643-Animals, pubmed-meshheading:9137643-Antigens, Helminth, pubmed-meshheading:9137643-Antigens, Plant, pubmed-meshheading:9137643-Ascaris, pubmed-meshheading:9137643-Blotting, Western, pubmed-meshheading:9137643-Chromatography, High Pressure Liquid, pubmed-meshheading:9137643-Conserved Sequence, pubmed-meshheading:9137643-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:9137643-Helminth Proteins, pubmed-meshheading:9137643-Molecular Sequence Data, pubmed-meshheading:9137643-Molecular Weight, pubmed-meshheading:9137643-Protein Structure, Secondary, pubmed-meshheading:9137643-S100 Proteins, pubmed-meshheading:9137643-Sequence Alignment, pubmed-meshheading:9137643-Sequence Homology, Amino Acid, pubmed-meshheading:9137643-Software
pubmed:year
1995
pubmed:articleTitle
Structural characteristics of the Ascaris allergen, ABA-1.
pubmed:affiliation
Department of Microbiology and Infectious Diseases, University of Calgary, Alberta, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't