. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 246 REPORTS FROM THE MBL GENERAL SCIENTIFIC MEETINGS Reference: Bio/. Bull. 187: 246-247. (October, 1994) Copper Induced Polymerization of Hemoglobin from the Ocean Pout, Macrozoarces americanus Thomas A. Borgese (Lehman College, CUNY), Sharon Bourke, Bernardo Frias, Donald Johnson, and John Harrington Hemoglobins that polymerize are not uncommon among amphibians, reptiles, and elasmobranchs, but are rare among teleosts and humans. They are useful models for the study of protein structure, function, and molecular evolutionar
. The Biological bulletin. Biology; Zoology; Biology; Marine Biology. 246 REPORTS FROM THE MBL GENERAL SCIENTIFIC MEETINGS Reference: Bio/. Bull. 187: 246-247. (October, 1994) Copper Induced Polymerization of Hemoglobin from the Ocean Pout, Macrozoarces americanus Thomas A. Borgese (Lehman College, CUNY), Sharon Bourke, Bernardo Frias, Donald Johnson, and John Harrington Hemoglobins that polymerize are not uncommon among amphibians, reptiles, and elasmobranchs, but are rare among teleosts and humans. They are useful models for the study of protein structure, function, and molecular evolutionary rela- tionships. The freshwater teleost Hoplias malabarica (1), the marine teleost Lophius americanus (2), and the clown fish, Am- phiprion (3) are the only bony fishes reported to have hemoglo- bins that polymerize. Hoplias and Lophius polymerize by form- ing intermolecular disulfide bonds, while the polymerization mechanism for the clown fish is, as yet, unknown. Among hu- mans, hemoglobins Ta-Li, Mississippi, and Porto Alegre (4, 5, 6) have a single mutation involving the substitution of a cysteine residue at different loci on the globin chain. We now report that the ocean pout has a single hemoglobin with six sulfhydryl groups per tetramer and polymerizes, in vitro, after oxidation with po- tassium ferricyanide (K,Fe(CN)6) or cupric chloride (CuCl:). Procedures for hemoglobin purification by DE-52 cellulose chromatography, molecular weight estimations by gel filtration on G-100 columns, and urea gel electrophoresis for globin sub- unit analysis have been described (2). Hemoglobin was incubated with a two- to threefold molar excess of CuCU for 15 min in an ice bucket. The excess copper was removed by dialysis or by gel filtration from Sephadex G-25 columns equilibrated with M , buffer, pH Thereafter 20-40 mg of the hemoglobin was applied to and eluted from G-100 columns. One-mi fractions were collected and the absorbance of each measured at 540 nm. The approx
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