873905

Source:http://linkedlifedata.com/resource/pubmed/id/873905

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0014442, umls-concept:C0026336, umls-concept:C0087111, umls-concept:C0439792, umls-concept:C1511726, umls-concept:C1533148
pubmed:issue	13
pubmed:dateCreated	1977-8-25
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/2985121R
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Enzymes
pubmed:status	MEDLINE
pubmed:month	Jul
pubmed:issn	0021-9258
pubmed:author	pubmed-author:FriedelEE, pubmed-author:PettigrewD WDW
pubmed:issnType	Print
pubmed:day	10
pubmed:volume	252
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	4546-51
pubmed:dateRevised	2006-11-15
pubmed:meshHeading	pubmed-meshheading:873905-Allosteric Regulation, pubmed-meshheading:873905-Computers, pubmed-meshheading:873905-Enzymes, pubmed-meshheading:873905-Kinetics, pubmed-meshheading:873905-Models, Biological, pubmed-meshheading:873905-Models, Chemical, pubmed-meshheading:873905-Osmolar Concentration, pubmed-meshheading:873905-Protein Conformation
pubmed:year	1977
pubmed:articleTitle	Treatment of enzyme kinetic data. Extension of the concerted allosteric model to the two-substrate case.
pubmed:publicationType	Journal Article, Research Support, U.S. Gov't, P.H.S.