On the analogy in the structure of the spleen green heme protein and granulocyte myeloperoxidase.
The molecular structure of the spleen green heme protein was reinvestigated by gel-permeation, SDS-polyacrylamide gel electrophoresis, and amino acid analysis. The results showed that the enzyme is a tetramer (Mr 1.5 X 10(5)) with two heavy subunits (Mr 6 X 10(4) with a single prosthetic group per subunit) and two light subunits (Mr 1.5 X 10(4)), and that the tetramer structure is maintained by disulfide bond(s). The amino acid composition of the spleen green heme protein is similar to that of granulocyte myeloperoxidase. The present results contradict the data of Davis and Averill [(1981) J. Biol. Chem. 256, 5992-5996], who reported the enzyme as a monomeric peroxidase with an Mr of 57 000.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002850:Chromatography, Gel; D004220:Disulfides / Q000032:analysis; D004229:Dithiothreitol / Q000494:pharmacology; D004285:Dogs; D004591:Electrophoresis, Polyacrylamide Gel; D006098:Granulocytes / Q000201:enzymology*; D006801:Humans; D007460:Iodoacetamide / Q000494:pharmacology; D046911:Macromolecular Substances; D009195:Peroxidase / Q000032:analysis*; D013154:Spleen / Q000201:enzymology*
D000596:Amino Acids; D004220:Disulfides; D046911:Macromolecular Substances; D009195:Peroxidase; D004229:Dithiothreitol; D007460:Iodoacetamide