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• W2005657910 abstract "The red cells of the arcid clam Anadara ovalis contain two electrophoretically distinct hemoglobins: Hb Major (Hb Ma) and Hb Minor (Hb Mi). The major component consists of two electrophoretically indistinguishable tetramers each composed of two heterodimers; the minor hemoblogin is a homodimer whose subunits are different from the tetramer. Functionally, Hb Ma has a higher P50, exhibits a concentration dependent oxygen affinity, has significant ligand cooperativity (n = 2.0), lacks a Bohr effect and is unaffected by ATP. HB Mi has a P50 which is lower and independent of hemoglobin concentration, shows appreciable cooperativity (n = 1.4) and exhibits no heterotropic effects. Both Hb Ma and Mi are resistant to dissociation in the presence of 1.0 M NaI, NaCl and guanidine-HCl but dissociate to monomers when converted to the aquamet but not the cyanmet derivative. The dissociation is completely inhibited by mercaptoethanol. The large number of reactive -SH groups (10-13 per tetramer) suggests that the monomerization is mediated by intra-subunit disulfide bridge formation." @default.
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• W2005657910 date "1987-01-01" @default.
• W2005657910 modified "2023-09-27" @default.
• W2005657910 title "Anadara ovalis hemoglobins: Distinct dissociation and ligand binding characteristics" @default.
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• W2005657910 doi "https://doi.org/10.1016/0305-0491(87)90191-x" @default.
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