title: Structure of extracellular hemoglobin from the brine shrimp Artemia salina.
abstract: 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 Mr 150,000. 2. Crosslinking by glutardialdehyde resulted in the appearance of a band corresponding to a molecular mass twice that of a polypeptide chain. 3. Limited trypsinolysis gave eight proteolytic bands corresponding to submultiples 8/9-1/9 of a polypeptide chain. 4. We conclude that a molecule of Artemia hemoglobin is composed of two single polypeptide chain subunits and that each subunit consists of nine structural units roughly equal in size.
authors.affiliation: Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel-Aviv University, Israel.
authors.forename: A
authors.initials: A
authors.lastname: Azem
authors.forename: E
authors.initials: E
authors.lastname: Daniel
mesh_terms: D000818:Animals; D001156:Artemia / Q000737:chemistry*; D004591:Electrophoresis, Polyacrylamide Gel; D006454:Hemoglobins / Q000737:chemistry* / Q000302:isolation & purification; D015394:Molecular Structure; D014461:Ultracentrifugation
chemical_list: D006454:Hemoglobins