Structure of extracellular hemoglobin from the brine shrimp Artemia salina

1. 1. Hemoglobin from the brine shrimp Artemia salina, purified by ultracentrifugation and preparative gel electrophoresis in non-denaturing medium, gave in sodium dodecyl sulfate-polyacrylamide gel electrophoresis a single band corresponding to a polypeptide chain with M_r 150,000. 2. 2. Crosslinking by glutardialdehyde resulted in the appearance of a band corresponding to a molecular mass twice that of a polypeptide chain. 3. 3. Limited trypsinolysis gave eight proteolytic bands corresponding to submultiples 8 9- 1 9 of a polypeptide chain. 4. 4. We conclude that a molecular of Artemia hemoglobin is composed of two single polypeptide chain subunits and that each subunits consists of nine structural units roughly equal in size.