The Action of Nitrites on Blood

Marshall, Wilfrid; Marshall, Charles R.

doi:10.1016/s0021-9258(17)41605-x

Cited by 38 publications

(7 citation statements)

References 20 publications

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“…The complex formed (Fig. 1) is similar to the nitrite-methemoglobin complex reported by Marshall and Marshall (1945). They found that the height of the shoulders at 530-540 and 570-580 µ in the methemoglobin absorbancy spectrum varied with the amount of nitrite added to methemoglobin and concluded that the compound formed was an ionic complex of nitrite and methemoglobin.…”

Section: Methodssupporting

confidence: 80%

Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5^*

Fox¹,

Thomson²

1963

Biochemistry

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Section: Methodssupporting

confidence: 80%

Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5^*

Fox¹,

Thomson²

1963

Biochemistry

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“…The peak positions for nitrosylhemoglobin are at 545 nm and 565 nm and the minimum between these two peaks is less pronounced than with oxyhemoglobin. The similarity between the nitrosylhemoglobin and oxyhemoglobin spectrum was noted in an early publication (14) although other work (15,16) has placed the nitrosylhemoglobin maxima at different wavelengths.…”

Section: Resultsmentioning

confidence: 64%

Hemoglobin. Isolation and chemical properties

Russo¹,

Sorstokke²

1973

J. Chem. Educ.

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“…Cytochrome c, which will be discussed in Chapter VIII, belongs to this category. Another compound of this type is heUconibin, which was detected in 1876 by Sorby in the hepatopancreas of the snail Helix. Helicorubin has been studied by Krukenberg, MacMunn ("enterohematin"), Dastre and Floresco, Dhere and Vegezzi {587; here the earlier literature is reviewed), Anson and Mirsky {(il), and Roche and Morena {2320).…”

Section: Denatured Globin Hemochromementioning

confidence: 99%

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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The Action of Nitrites on Blood

Cited by 38 publications

References 20 publications

Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5^*

Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5^*

Hemoglobin. Isolation and chemical properties

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

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The Action of Nitrites on Blood

Cited by 38 publications

References 20 publications

Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5*

Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5*

Hemoglobin. Isolation and chemical properties

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

Contact Info

Product

Resources

About

Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5^*

Formation of Bovine Nitrosylmyoglobin. I. pH 4.5-6.5^*