Molecular and genetic structure of multiple hemoglobins in the eelpout, Zoarces vivparus L

Six major hemoglobin components are present in the teleostean fish Zoarces viviparus L. Biochemical characterization has led to a molecular model for the polypeptide chain composition of the individual hemoglobins. Only three different chains are involved. They are determined by three different structural loci, as indicated by the genetic variation of the electrophoretic hemoglobin pattern observed in natural populations. Hemoglobins occur that, despite identical chain compositions, have different electrophoretic mobilities. This may be due to a mechanism, known from man, where part of the hemoglobin is blocked by a hexose.