Animal Pigments

Lemberg, R.

doi:10.1146/annurev.bi.07.070138.002225

Cited by 11 publications

(2 citation statements)

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“…The correct structure of the bile pigments was recognized comparatively late (in 1931) and most of the earlier reviews {882,883, 1597,1602) are now mainly of historical value, although they contain much interesting detail. In Fischer's book {861) the synthetic work which led to the recognition of the correct structure of bilirubin is fully dealt with, but other bile pigment classes are treated less adequately and considerable progress has been made in this field since 1938. This later development has been onh' incompletely reviewed (860,1534,1683,2990).…”

Section: Structurementioning

confidence: 99%

“…HEMATIN ENZYMES, I. CYTOCHROME SYSTEM linkages to the iron. Lemberg (1683) pointed out that the heraochrome structure of cytochrome c can only be explained by assuming that the heme is bound in a crevice of the protein molecule, in which it is firmly anchored by the thioether linkages. Theorell assumes that this rigid structure explains why cytochrome c does not react with oxygen or carbon monoxide.…”

Section: Spectroscopic Observations On Cytochromesmentioning

confidence: 99%

See 1 more Smart Citation

Hematin compounds and bile pigments; their constitution, metabolism, and function, by R. Lemberg and J.W. Legge.

Legge¹,

Lemberg²

1949

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II. METHODS or INVESTIGATION* Only the naturally occurring hile pigments of type IXa are discussed.* .\11 tlie al).s()r[)ti()ii curves of the "hiliverdiiis" in Heihiieyers hook (121-i) are ohviously tliose of niixtiirt's of liiliverditi witli hiliruliiii (pages 1(51, 1()7) and other * The term K-urobilin is, however, used by the Fischer school to denote a mixture of side chain isomerides of mesobilene-(b) in contradistinction to mesobilene-(b) IXa.* It is not certain, however, whether the albumin is the only plasma protein able to combine with hematin (c/. Miller and Ailing, 191f9a).* Keilin and Smith {1502a) have been unable to confirm the results of Virtanen and Laine.XII. HEMOGLOBIN CATABOLISM, II * Cf., however, Bittner and Watson {28-3a). CHAPTER XIII FORMATION OF HEMOGLOBIN AND SYNTHESIS OF PORPHYRINSIN THE ANIMAL BODY * The hemoglobin found occasionally in some species of Daphnia (Fox,937aa) does not appear to have an essential physiologic function, although, like the hematin compounds mentioned above, it is passed on in parthenogenetic eggs. Even the chlorocruorin or erythrocruorin of serpulimorphid worms does not appear to be essential (Fox, 937a).Glaucobilin. See Mesobiliverdin. Globan, 211. See also Globin (denatured). Globin, denatured, 240, 258 combination with heme, 232 electrometric titration, 255 in erythrocytes, 525 isoelectric point, 255 renaturation, 259 Globin, native, 230, 258, 568 amino acids. See Hemoglobin. combination, with hematins, 239 with metalloporphyrins, 240 with porphyrins, 240 denaturation, 255 ff. 734 SUBJECT INDEX Globin native (contd.) electrometric titration, 255 differential of globin and hemiglobin, 244 fate in hemogIol>in breakdown, 548, 568 frictional ratio, 250 isoelectric point, 255 molecular weight, 250 oxidation, in autoxidation of hemoglobin, 390 in denaturation, 395, 478 preparation, 258 specificity, 321. See also Hemoglobin. synthesis in vivo, 610 Glutathione as anticatalase, 412 and choleglobin formation, 477, 478, 517 and dehydroascorbic acid, 470, 517, 518 in erythrocyte, 516, 522, 619 and hem/globin, 522 as substrate of cytochrome c, 376 Glycine, in porphyrin s\nthesis, 637 Gmelin reaction, 109, 112 (table), 116, 138 Green hemins, 201, 456, 490. See also Chlorophyll hemins, Pheophorbide kemin, Verdochemochrome.

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