Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1995-4-13
pubmed:abstractText
Plasmid based yeast expression systems have been developed for the high-level expression of the three human embryonic haemoglobins Gower I (zeta 2 epsilon 2), Gower II (alpha 2 epsilon 2) and Portland (zeta 2 gamma 2). Physiochemical characterization of the three product haemoglobins show them to be in the 'native' state. Oxygen-binding studies show that, under what are usually considered physiological conditions, each of the embryonic haemoglobins shows a high oxygen affinity, coupled to a high degree of co-operativity. Allosteric modulation of the oxygen-binding properties of the three haemoglobins in response to organic phosphates and protons has been investigated. The various responses exhibited by the three haemoglobins are rationalized in terms of their amino acid sequences.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-1118015, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-1367213, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-1499566, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-234081, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-3322377, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-4515623, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-4555506, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-5443777, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-5472965, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-5528785, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-5789657, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-5789658, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-6171809, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-6172357, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-6254663, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-6452630, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-7332928, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-7411620, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-8041264, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-8141775, http://linkedlifedata.com/resource/pubmed/commentcorrection/7887890-8170931
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0264-6021
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
306 ( Pt 2)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
367-70
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Allosteric modulation of oxygen binding to the three human embryonic haemoglobins.
pubmed:affiliation
Biochemistry and Molecular Biology Research Group, School of Biological Sciences, University of Auckland, New Zealand.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't