Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1982-9-17
pubmed:abstractText
Precise immunological recognition of anti-viomycin antiserum at detailed parts in the structure of viomycin was studied by cross reactivities of the antiserum to viomycin and its ten analogs using an enzyme immunoassay of viomycin. The antiserum clearly recognized all minor modifications in the sixteen membered ring of viomycin, indicating that the antiserum clearly recognizes the whole structure of the sixteen membered ring. Recognition of the antiserum on the beta-lysine terminus was also examined showing that the antiserum was also recognized on this part. Thus, the anti-viomycin antiserum was deduced to recognize the whole structure of viomycin, from which the deduction was made that the anti-viomycin antibodies in the antiserum must possess cavities fitting the whole structure of viomycin. The crystal dimensions of viomycin are 13 A in length, 8 A in width, and 7 A in depth. Thus, the high dimensional structure of the binding sites of the anti-viomycin antibodies was deduced to possess cavities of a similar size to that of viomycin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1601-5
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
High dimensional structure of the antigen-binding site of anti-viomycin immunoglobulin analyzed by enzyme immunoassay.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't