Structural Characterization of Cross-Linked Hemoglobins Developed as Potential Transfusion Substitutes
Abstract
Structural and functional studies of chemically modified hemoglobins have been done in an effort to find reagents and conditions that are suitable to produce cross-linked hemoglobin derivatives that would be suitable for use as a cellular substitutes for the transfusions of erythrocytes. The effects of modifying hemoglobin with five different dicarboxylic bis(methyl phosphate) reagents provided by Professor Ronald Kluger have been examined by ion exchange separation of hemoglobin products, globin chain separation, peptide pattern analysis, and oxygen equilibrium measurements. These reagents were found to react only with beta-1val, beta-821ys, alpha-1val, alpha-991ys, and alpha-1391ys but to varying extent depending on the conformational state of the hemoglobin. Both cross-linked and uncross-linked products have been found. Several have reduced oxygen affinities. The hemoglobins present in Batch 11 of DBBF-Hb from Baxter was examined by the same chromatographic and structural procedures in order to determine the extent and structural basis of the heterogeneity of this product.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 30, 1990
- Accession Number
- ADA225232
Entities
People
- Richard T. Jones
Organizations
- Oregon Health & Science University