Abstract
The paper discusses the functional properties of hemoglobins intramolecularly crosslinked with tricarboxylic and dicarboxylic acids. Intramolecular crosslinks are produced either between the α99 or β82 lysines. The increasing length of the crosslink between the β subunits from 4 to 14 carbon atoms progressively decreases the oxygen affinity of hemoglobin. Preliminary data suggest that the same may be true for the crosslinks between α subunits. The triester of benzene-tricarboxylic acid produces very homogeneous β-β crosslinked hemoglobins, with low oxygen affinity.
| Original language | English (US) |
|---|---|
| Pages (from-to) | A84 |
| Journal | Artificial Cells, Blood Substitutes, and Immobilization Biotechnology |
| Volume | 22 |
| Issue number | 5 |
| State | Published - Nov 1 1994 |
| Event | Proceedings of the 11th Congress of the International Society for Artificial Cells, Blood Substitutes and Immobilization Biotechnology, (ISABI) - Boston, MA, USA Duration: Jul 24 1994 → Jul 27 1994 |
ASJC Scopus subject areas
- Biotechnology
- Biomedical Engineering