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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
|
pubmed:dateCreated |
1981-12-21
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pubmed:abstractText |
Stroma-free hemoglobin solutions present some drawbacks when used as blood substitutes, essentially because the hemoprotein has a low vascular retention, due to its small hydrodynamic volume. Covalent coupling of the protein with dextran derivatives artificially increases its size and affords polymeric conjugates whose oxygen-binding properties (Barcroft's curve, Hill coefficient) depend on the molecular weight.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:issn |
0014-4754
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
|
pubmed:pagination |
884-6
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:6169540-Chemical Phenomena,
pubmed-meshheading:6169540-Chemistry,
pubmed-meshheading:6169540-Dextrans,
pubmed-meshheading:6169540-Hemoglobins,
pubmed-meshheading:6169540-Humans,
pubmed-meshheading:6169540-Molecular Weight,
pubmed-meshheading:6169540-Oxidation-Reduction,
pubmed-meshheading:6169540-Oxygen
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pubmed:year |
1981
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pubmed:articleTitle |
Preparation and oxygen binding properties of soluble covalent hemoglobin-dextran conjugates.
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pubmed:publicationType |
Journal Article
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