Lactic Dehydrogenase of Yeast

Bach, S. J.; Dixon, Malcolm; Zerfas, L. G.

doi:10.1038/149048a0

Cited by 17 publications

(5 citation statements)

References 3 publications

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“…resistant to autolysis than the yeasts used by the American workers. Similar differences between Delft and Manchester yeasts have been noted by Bach, Dixon & Zerfas (1942 in the preparation of lactic dehydrogenase. Prof. F. Dickens (private communication) has experienced similar difficulties in extracting hexokinase from Distillers Company Ltd. baker's yeast.…”

Section: Purification Of Hexokinasesupporting

confidence: 79%

Purification of yeast hexokinase and its reaction with ββ′-dichlorodiethyl sulphide

Bailey

Webb

1948

Biochemical Journal

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Section: Purification Of Hexokinasesupporting

confidence: 79%

Purification of yeast hexokinase and its reaction with ββ′-dichlorodiethyl sulphide

Bailey

Webb

1948

Biochemical Journal

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“…Cytochrome 62. A water-soluble cytochrome b has been found in purified yeast lactic acid dehydrogenase, which is quite different from the lactic acid dehydrogenase of mammals; it has been called cytochrome b2 112,113; Haas and co-workers, 1077). Its absorption bands lie at 560.5 m^and 530 m^, but its concentration in the yeast cell is too small for spectroscopic observation.…”

Section: Cytochromes Bmentioning

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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“…clearly by comparing the spectrum of aldehyde oxidase (Figs. 3, 4) with that of the crystalline lactic oxidase isolated from yeast by Morton and Appleby (51) and known to contain FMN and cytochrome bz (52,53) in a ratio of 1 : 1 (Fig. 5).…”

Section: B Aldehyde Oxidase (Liver)mentioning

confidence: 99%

Nature and Function of Metalloflavoproteins

Mahler¹

1956

Advances in Enzymology - And Related Areas of Molecular Biology

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Lactic Dehydrogenase of Yeast

Cited by 17 publications

References 3 publications

Purification of yeast hexokinase and its reaction with ββ′-dichlorodiethyl sulphide

Purification of yeast hexokinase and its reaction with ββ′-dichlorodiethyl sulphide

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

Nature and Function of Metalloflavoproteins

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