Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-3-30
pubmed:abstractText
Hydroxymethylbilane synthase (porphobilinogen deaminase) was purified to apparent homogeneity from Escherichia coli. The enzyme is a monomer of Mr approx. 40,000. The Km for porphobilinogen and relative Vmax. values have been obtained at various pH values over the range 6.2-8.8, enabling pK values for ionizable groups important for activity to be determined. The N-terminal amino acid sequence is presented.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-1056172, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-4539746, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-4542566, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-4680711, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-6433896, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-6712591, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-6769048, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-6796041, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-6974651, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-7213640, http://linkedlifedata.com/resource/pubmed/commentcorrection/3548707-7354069
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
240
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
273-6
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't