Linked Life Data

8318609

Source:http://linkedlifedata.com/resource/pubmed/id/8318609

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-7-30
pubmed:abstractText
Human oxyhemoglobin reacts with mellitic dianhydride to produce a modified protein which shows a reduced oxygen affinity over a wide pH range, a reduced but significant cooperativity, a reduced Bohr effect and no response to the allosteric effectors: chloride, clofibric acid or inositol hexaphosphate. The amount of crosslinking in the modified hemoglobin is approximately 22% suggesting promise as a blood substitute. Reaction of deoxyhemoglobin with mellitic dianhydride produces a modified protein with reduced response to clofibric acid and a decrease in oxygen affinity in the presence of inositol hexaphosphate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1055-7172
pubmed:author
pubmed:issnType
Print
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
153-62
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The functional properties of hemoglobin modified with mellitic dianhydride: possible applications as a blood substitute.
pubmed:affiliation
Department of Chemistry and Biochemistry, California State University, Los Angeles 90032.
pubmed:publicationType
Journal Article