Ability of Blood with Altered Affinity and Hemoglobin Solutions to Deliver Oxygen.
Abstract
We compared O2 delivery in isolated hearts (1) by red blood cells (RBC) as a function of oxygen dissociation curve position (P50) and (2) by purified hemoglobin in direct comparison to RBC. Hearts were retrograde perfused and performed isometric work by compressing a left ventricular fluid-filled balloon. A right shift of the oxygen dissociation curve (due to incorporation of inositol hexaphosphate into red cells) improved function and myocardial oxygen consumption. Hemoglobin, at equivalent hemoglobin concentration and P50, was indistinguishable from RBC in this model. These findings have important relevance to the Army's blood program. We also studied the effect of a new allosteric modifier of hemoglobin function (termed RSR-13), which powerfully shifts the oxygen dissociation curve to the right, on cardiac output and its distribution in lightly anesthetized rats. We found no effect on either cardiac output or on absolute or relative blood flow to any organ. This finding is quite surprising finding and runs counter to standard physiologic dogma and most previous work. As such it has potentially important implications for basic physiologic concepts but requires further study.
Document Details
- Document Type
- Technical Report
- Publication Date
- Apr 01, 1995
- Accession Number
- ADA308057
Entities
People
- Gosta Berlin
- Keith E. Challoner
- Robert D. Woodson