Reexamination of the Polymerization of Pyridoxylated Hemoglobin with Glutaraldehyde
Abstract
Use of hemoglobin solutions as plasma expanders offers the desirable properties of low viscosity, oncotic activity, and oxygen and carbon dioxide transport. Extracellular hemoglobin, however, binds oxygen much more tightly than intracellular hemoglobin due, in part, to the loss of 2,3- diphosphoglycerate and to the lower pH of the plasma. This defect may be adequately overcome with pyridoxal 5-phosphate (PLP) as well as with a number of other reagents. Another disadvantage in the use of hemoglobin solutions for resuscitation therapy lies in the short circulating half-life of native hemoglobin, which is considered to be due to the glomerular filtration of the dimeric form of hemoglobin. To overcome this limitation, various means have been proposed such as encapsulation, or chemical modification to form intramolecular and/or intermolecular cross-links. Intratetrameric cross-linking with disubstituted aspirin derivatives prevents dimerization, as do the dextran dialdehydes, glycoaldehyde, and 2-nor-2-formylpyridoxal 5-phosphate. A common means used to extend the vascular retention of hemoglobin solutions has been by polymerization with glutaraldehyde (GLUT), which forms intra- and inter- molecular cross-linked hemoglobin that retards the rate of renal clearance. (jg)
Document Details
- Document Type
- Technical Report
- Publication Date
- Jan 01, 1990
- Accession Number
- ADA223224
Entities
People
- G. L. Moore
- M. A. Marini
- R. G. Jessee
- R. M. Fishman
- S. M. Christensen
Organizations
- Letterman Army Hospital