Hemoglobins from Ascaris lumbricoides*

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Abstract
Purified hemoglobins A1 and A2 (cf. J. Biochem. (Tokyo) 52,290(1962)) showed the following physlochemical properties: affinity constant (the concentration of the compound required for 50% combination), for ethylisocyanide, A1 9 x 10-7and A2 3.9 x 10-5; for cyanide, A1 9.5 x 10-2 and A2 5.0 x 10-2 [image]; the heme-heme interaction coefficient in the oxygenation reaction, A1 1.7 and A2 0.7. Both A1 and A2 exhibited no Bohr effect. The A1 and A2-ethylisocyanide complexes gave an absorption band at 428 m[mu], and the A1- and A2-cyanide complexes at 534 and 561 m[mu]. The cyanide complexes were converted during dialysis at pH 7.0 to resp. cyanide methemoglobins (417,543 m[mu]), which could be reduced by Na2S2O4 to A1 and A2, resp.

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