736 



SUBJECT INDEX 



Henioglohin (coritd.) 



hemes, arrangement in, 251 

 interaction between hemes, 260, 263- 

 270, 286, 291-295 

 constant a, 265, 268, 270, 292 

 functional importance of, 326, 328 

 pathway of, 292 

 intermediates, attempts of direct 

 discovery, 271 

 between hemoglobin and hemo- 

 globin, 270 

 between hemoglobin and oxy- 

 hemoglobin, 263-269 

 between oxyhemoglobin and sulf- 

 liemoglobin, 494, 497 

 in complicated systems, 271 S. 

 iron content, 213 

 isoelectric point, 246 

 kinetics, methods, 278. .See also 

 individual compounds, 

 of hemoglobin reactions in ery- 

 throcyte, 284 

 linkage, of iron to O., and CO, 231 

 of hematin cari)oxyls to protein, 



240-242, 244, 245 

 of iron to gloliin, 231 

 of iron to imidazole, 217, 224, 232- 



239, 256, 276, 292-294 

 of prosthetic group and protein, 230 

 methemoglobin and its compounds. 



See Hemiglohin below, 

 molecular weight, 245, 246, 311, 312, 

 313 ftalde), 314, 320 

 dissociation of molecule into 

 halves, 246, 250, 252 

 nomenclature, 208, 209 (table) 

 normal, 297, 605 



life curve of, 606 

 as oxidase, 338, 339, 342, 388, 392- 



396, 482, 515 

 oxidation-reduction equilibria, 261, 

 270, 274 

 effect of pH on, 275 

 oxygen capacity, 213 > 



oxylabile groups, 232, 233, 237 



(table), 238, 275-277 

 as peroxidase, 338, 403, 437 

 of Pelromi/zon, 312, 313 (table), 315 

 proteolytic degradation, 231 

 reduced hemoglobin and its com- 

 pounds. See Hemoglobin below, 

 in root nodules, 306, 311, 449, 654 

 shape of molecule, 248, 320 



Hemoglobin (confd.) 

 solubility, 318, 320 

 specificity, 305, 308, 315 ff., 321 ff. 

 See also Erylhrocruorins, Myo- 

 hemoglobin. Hemoglobin (fetal). 

 and absorption spectra, 308, 322 

 sulfhydryl groups, 254, 258 

 surface properties, 320 

 synthetic hemoglobins, 239 

 transformation, into methemal- 

 bumin, 574, 576 

 into porphyrins, 592, 593 ff. 

 and urea, 246 

 x-ray analysis, 248, 252 

 hemoglobin anabolism 

 and catabolism, 625 

 from nuclear material, 605, 613 

 rate of, 623 



requirements for, 607 ff. 

 amino acids, 610 

 minerals, 617 ff. 

 pyrrole compounds, 608, 609 

 vitamins, 612, 613 ff. 

 self-regulation, 624 ff. 

 theory of, 637 ff. 

 hemoglobinemia, 5.33, 534, 536 

 hemoglobinuria, 533-535 



and kidney damage, 534, 535 



hemjglol)in, 218, 394. See also Hemi- 

 globin formation. 

 absorption spectra, 227, 228 (table) 

 compounds. See below, 

 differential titration of hemzglobin 



arid globin, 244 

 dissociation constants, 236 ff., 237 



(table), 276 

 effect on oxyhemoglobin dissociation, 



273, 519 

 in normal erythrocyte, 518 

 estimation, 297-299, 302 

 kinetics, of combination with 

 cyanide, 285 

 of reduction, 285 

 linkage imidazole-iron in, 236-239 

 magtietochemistry, 218 

 in oxyhemoglobin preparations, 211 

 pleochroism of crystals, 251 

 reduction, in erythrocyte, 515-518, 

 522 

 by ascorbic acid, 517 

 by glutathione, 516 

 in root nodules, 449 



