Linked Life Data

911884

Source:http://linkedlifedata.com/resource/pubmed/id/911884

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1977-12-29
pubmed:abstractText
Neuraminidase was isolated by proteolysis of the X7-(F1) (HON2) strain of influenza virus, and purified by gel filtration. The molecule contained a total of 46% (w/w) carbohydrate. The Mr was estimated as 152 500 (sedimentation diffusion) and 147 000 (sedimentation equilibrium). In 6 M guanidine-HCl the molecular weight was halved to 66 000 (sedimentation equilibrium). After irreversible reduction and blocking of sulphydryl groups the molecular weight was halved again to 33 500 (sedimentation equilibrium). These results confirm the tetrameric model of neuraminidase structure. They also provide strong evidence that the tetramer is composed of two disulphide linked dimers, themselves associated by non-covalent linkages. Theoretical considerations based on this model predict that assembly of the molecule must be accompanied by allosteric conformational changes in the subunits. The high carbohydrate content was thought to explain the discrepancy between the molecular weight values for the neuraminidase polypeptide obtained by different methods, and also the exceptional resistance of the molecule to digestion by proteolytic enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
495
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
58-70
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Structural and composition of the N2 neuraminidase of influenza virus. Effect of carbohydrate content on the validity of molecular weight estimations.
pubmed:publicationType
Journal Article