Die Niere als Blutzerstörendes Organ

Bingold, K.

doi:10.1007/bf01812705

Cited by 20 publications

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“…In fact, the catalase may have offered some protection because a portion of the partially purified pigment underwent oxidative destruction accompanied by protein denaturation and formation of the green verdohemochromogen. Bingold (1933) demonstrated that catalase did protect oxyhemoglobin from oxidation by high concentration of H202. Brooks (1935) found the rate of oxidation of hemoglobin to methemoglobin in buffered, laked, defibrinated blood at different oxygen pressures to be proportional to the concentration of reduced hemoglobin.…”

Section: Discussionmentioning

confidence: 99%

Role of Bacteria in the Oxidation of Myoglobin12

Robach¹,

Costilow²

1961

Applied Microbiology

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The addition to steaks of cell suspensions of a number of aerobic bacteria and of Saccharomyces cerevisiae greatly increased the rate of discoloration. Low inocula resulted in the more rapid appearance of the brown color of metmyoglobin, whereas high cell populations quickly produced the purple color of myoglobin. Sonically treated suspensions of Pseudomonas geniculata produced similar changes in surface color but less rapidly. No such effect was observed with Lactobacillus plantarum. The visible changes in color were found to be associated with the oxygen demand of the surface tissue including, of course, the demand of any contaminating microorganisms. Inhibitors of respiratory activity inhibited the rate of discoloration under normal atmospheric conditions. However, when the oxygen level in the atmosphere was reduced, the inhibitors had no significant effect. In an oxygen-free atmosphere, the steak surfaces were the purple color of myoglobin; at 10 mm oxygen pressure, the pigment was oxidized to metmyoglobin and the surface was brown in color. No bacterial activity was necessary for pigment oxidation under low oxygen pressures. Addition of dilute solutions of glucose oxidase resulted in rapid oxidation of the meat pigment to metmyoglobin both in extracts and on steak surfaces. More concentrated solutions resulted in further oxidation as evidenced by the appearance of a green color. Horseradish extract with a high peroxidase activity added with H202 resulted in rapid oxidation of the pigment but neither were very effective alone, although H202 did result in a browning reaction in aged steaks. It is concluded that the primary role of the bacteria in meat discoloration is in the reduction of the oxygen tension in the surface tissue. The implications of the data are discussed and a possible mechanism of myoglobin oxidation is proposed. I Journal article no. 2791, Michigan Agricultural Experiment Station.

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Section: Discussionmentioning

confidence: 99%

Role of Bacteria in the Oxidation of Myoglobin12

Robach¹,

Costilow²

1961

Applied Microbiology

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“…Pentdyopent. In a series of papers Bingold (269)(270)(271)(272)(273)278) has claimed that pentdyopent (cf. Chapter IV, and Chapter X, Section 9.)…”

Section: 23mentioning

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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“…It has been suggested by Bingold (1933) that the function of catalase within corpuscles is the protection of haemoglobin against oxidative destruction by H202 formed in different tissues, especially in the kidney. That endoerythrocytic catalase, under certain experimental conditions, is capable of protecting haemoglobin from oxidation by H202 to methaemoglobin can easily be demonstrated.…”

Section: The Possible Function8 Of Catala8ementioning

confidence: 99%