Molecular Heterogeneity of Pyridoxalated-Polymerized Hemoglobin.

Abstract

The molecular heterogeneity of solutions of pyridoxalated polymerized hemoglobin has been examined in a stepwise manner by using high pressure liquid chromatography (HPLC), electrophoresis and incorporation of C14 pyridoxal phosphate. Starting hemoglobin contained several major and several minor protein components, all of which appear to be pyridoxalated, some perhaps multiple times. The subsequent polymerization of this mixture with glutaraldehyde produces an extremely heterogeneous mixture of distinct protein species. We estimate the number of molecular species to be in the hundreds since there are too many to resolve by isoelectric focusing (IEF) or TSK-HPLC. However, SDS-PAGE electrophoresis reduced 75% of the hemoglobin to the same monomer form as starting hemoglobin. This heterogeneity will add to the complexity of developing a modified hemoglobin as a blood substitute. Keywords: Blood proteins; Electrophoresis; Blood chemistry;' Blood analysis.

Open PDF

Document Details

Document Type
Technical Report
Publication Date
Dec 04, 1986
Accession Number
ADA176551

Entities

People

  • Gerald L. Moore
  • Jerry A. Tillotson
  • Mary E. Moore

Organizations

  • Letterman Army Hospital

Tags

Communities of Interest

  • Biomedical

DTIC Thesaurus Topics

  • Albumins
  • Amino Acids
  • Biological Sciences
  • Biomedical And Dental Materials
  • Blood Proteins
  • Blood Substitutes
  • Cellulose Acetates
  • Chemical Synthesis
  • Chemistry
  • Hemoglobin
  • High Pressure
  • Liquid Chromatography
  • Materials
  • Military Research
  • Molecular Weight
  • Polymeric Films
  • Pyridoxal Phosphate

Fields of Study

  • Chemistry

Readers

  • Cardiovascular Physiology
  • Molecular and Cellular Biochemistry