SUBJECT INDEX 



729 



Biliverdin (contd.) 



oocyan, in bird egg shells, 115, 506, 540 



oxidation by acidified oxyhemoglobin, 

 396 



reduction to bilirubin, 99, 545 



synthesis, 99, 100 (table), 101 



and urobilin, 545, 552 



uteroverdin, in dog placenta, 114, 506 

 Biliviolinoid substances, 107, 123, 570 

 Blood. See also Erythrocytes. 



carbon monoxide capacity, 485 



changes in stored, 528 



color index, 606 



iron, easily detachable, 482 

 nonhemoglobin, 484 



oxygen capacity, 485 



Caffeine 



compoimds with heme, 242, 244 

 with porphyrins, 241 

 with turacin, 241 

 Calliactin, 570 

 Carboxyhemoglobin, 215 



absorption spectrum, 226, 227, 228 

 (table) 

 infrared, 289 

 bond type, 215 



dissociation, 261 ff., 285, 286, 322 

 estimation, 302 



kinetics, of association, 281, 285, 286, 

 287 (table) 

 of dissociation, 281, 287 (table) 

 of reaction with O2, 283 

 light sensitivity, 216, 289 

 span, 289, 310 

 Catalase, 401, 403fiF. 

 anabolism, 627 

 and anions, 405, 442 

 and compounds, absorption spectra, 



405, 406 (table) 

 as antigen, 414 

 anticatalase, 412, 443 

 azide catalase, reaction with hydrogen 

 peroxide, 406 (table), 407, 412, 

 440ff. 

 bile pigment hematin in liver catalase, 



405, 413, 418, 499, 563 

 biological function, as peroxidative 

 enzyme, 417, 444 

 protection against H2O2, 416, 417, 652 

 catabolism, 569 

 coupled oxidation of alcohol, 418, 444 



Catalase (contd.) 

 and dithionite, 406 

 in erythrocyte, 418, 531 

 estimation, 410flF. 

 in evolution, 650, 651 

 inhibition, by destruction, 412 



of choleglobin formation, 476, 477 

 of hemoglobin formation in vivo, 418, 



521 

 of pseudohemoglobin formation, 490 

 of verdohemochrome formation, 468 

 inhibitors, 409 

 isolation, from erythrocytes, 404 



from liver, 404 

 Katalasefahigkeit (Kat.f.). 411 

 kinetics, 411 



magnetochemistry, 405, 406 (table) 

 mode of action, 439ff. 

 models, 401, 402 

 molecular weight, 414 

 occurrence, 415 

 and peroxidase, 401 

 philocatalase, 413, 443 

 protein, 414, 415 (table) 

 and respiration, 415, 416 

 transformation into protohemochrome, 

 406, 413 

 Chlorocruorins, 306, 308, 326 



absorption spectrum, 186 (table), 309 



(table) 

 biological function, 335 

 dissociation of oxychlorocruorin, 295 

 distribution, 307 (table) 

 in evolution, 326, 650 

 ferrichlorocruorin, 308, 309 (table) 

 protein, 314 (table), 315 

 and respiratory ferment, 362 

 Chloroma. See Choleglobin, Peroxidase 



(verdoperoxidase) , Protoporphyrin. 

 Chlorophyll 



chlorophyll b, 63, 571, 650 

 hemins derived from, 201, 403, 521, 608 

 in hemoglobin synthesis, 609 

 in photosynthesis, 1, 647, 650 

 porphyrins derived from, 648. See 

 also Etioporphyrin, Phylloerythrin, 

 Phylloporphyrin, Pyrroporphyrin, 

 Rhodoporphyrin. 

 and protoporphyrin, 651 

 structure, 5, 52 

 Choleglobin, 454 (table), 455, 472flF. 

 absorption sf)ectra, 454 (table), 472, 

 473 (table) 



