The Function of Human Hemoglobin. Salt Effects.
Abstract
A study was undertaken to confirm the Valtis and Kennedy salt effect (decrease in affinity of hemoglobin for oxygen with neutral salts) and to propose an explanation of the chemical mechanisms operating. Several concentrations of various neutral salts were added to whole blood which was depleted of 2,3-DPG and the p50 (the pO2 at 50% oxygenation, an inverse but direct measure of the oxygen affinity) was determined from oxyhemoglobin dissociation curves. The curves were obtained by tonometry of whole blood at 37 C and spectrophotometry. The salt effects (increase in p50 with various salts) seem to result from either a decrease in red cell pH or an increase in chloride concentration. (Author)
Document Details
- Document Type
- Technical Report
- Publication Date
- Dec 16, 1970
- Accession Number
- AD0719701
Entities
People
- Ben Dawson Jr.
- Clarence E. Swiggins
- Dickie W. Spurlock
- Thomas J. Ellis
Organizations
- United States Army Medical Research Laboratory