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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1976-8-23
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pubmed:abstractText |
Rabbit anti-human IgG antibody was mildly reduced in the presence of 10 mM 2-mercaptoethylamine and then coupled to beta-D-galactosidase [EC 3.2.1.23] from Escherichia coli using N,N'-o-phenylenedimaleimide. Human IgG and the anti-human IgG antibody-beta-D-galactosidase complex were successively adsorbed on Sepharose 4B binding rabbit anti-human IgG antibody. In this way amounts of human IgG as small as 5X10(-15) moles could be measured by determining the activity of beta-D-galactosidase bound to the Sepharose.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
423-5
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading | |
pubmed:year |
1975
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pubmed:articleTitle |
Enzyme-linked immunoassay. II. A simple method for synthesis of the rabbit antibody-beta-D-galactosidase complex and its general applicability.
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pubmed:publicationType |
Journal Article
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