Linked Life Data

6196055

Source:http://linkedlifedata.com/resource/pubmed/id/6196055

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1984-1-26
pubmed:abstractText
Stroma-free Hb solutions present some drawbacks when used as erythrocyte substitutes, mainly because the protein has a short in vivo half-life, due to its small hydrodynamic volume. Covalent coupling of oxyHb with dialdehyde-dextran (Mw congruent to 40 000; Mn congruent to 25 000) leads to adducts whose properties depend upon the pH of the condensations. At pH less than 9.6, many labile imine linkages are formed and the conjugates have a high molecular weight at the end of the reaction. In contrast, the final products obtained as pH increases from 9.6 to 10 contain a low-molecular-weight adduct in an increasing ratio; in this case the bond between dextran and Hb is stable and this stability is assumed to result from the rearrangement of a specific imine linkage formed at an NH2 site of Hb, into a ketoamine group (Amadori rearrangement). Dextran-Hb conjugates have oxygen-binding properties characterized by increased oxygen affinity, and decreased subunit cooperativity and alkaline Bohr effect, relative to unconjugated Hb. These differences become less as the time of condensation reaction decreases and seem to be due to modification of amine groups involved in the salt bridges that stabilize the deoxy form of the protein. Taking into account their oxygen-binding characteristics, the low-molecular-weight conjugates can be regarded as potential erythrocyte substitutes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
749
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
106-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Modification of human hemoglobin by covalent association with soluble dextran.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't