H�moglobine und andere H�moproteine

Kiese, Manfred

doi:10.1007/bf00669367

Cited by 6 publications

(8 citation statements)

References 102 publications

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“…Method of Kiese and Kurz (1954). These authors have confirmed the finding of Lemberg (1953) that the optimal water content of the acetone-HCl extract lies between 20 and 30 p.c.…”

Section: Methods Ofsupporting

confidence: 80%

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Porphyrins With Formyl Groups V

Lemberg¹,

Bloomfield²,

Caiger³

et al. 1955

Aust J Exp Biol Med

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“…Method of Kiese and Kurz (1954). These authors have confirmed the finding of Lemberg (1953) that the optimal water content of the acetone-HCl extract lies between 20 and 30 p.c.…”

Section: Methods Ofsupporting

confidence: 80%

“…Thawing of frozen, mince. Eapid thawing of frozen mince, suggested by Kiese and Kurz (1954), offered no distinct advantage over slow thawing at 4° C. Method B, gave 107±I4 mg. per kg. of dry mince, E III/IV=1.81±0.02, slow thawing 102±7 mg. of R III/IV=1.89±0.07.…”

Section: Varutions Of Methodmentioning

confidence: 99%

Porphyrins With Formyl Groups V

Lemberg¹,

Bloomfield²,

Caiger³

et al. 1955

Aust J Exp Biol Med

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“…The details of its spectrum, however, depend on the conditions to a far greater extent than the absorption spectrum of protohaemochrome, and this has led to some confusion. Thus " Warburg and Gewitz (1951) reported that a band resembling in position that ol" protohaemochrome is formed on reduction with dithionite, while no such band was observed by Rawlinson and Hale (1949), Lemberg (1935) or Kiese and Kurz (1954); again Kiese and Kurz observed a weak band at 534 m^. not found by the other authors.…”

Section: Haemin Amentioning

confidence: 85%

“…Poi'phyrin a is converted into haemin a and the latter reconverted into the porphyrin. This allows the comparison of the haemin a, reconstituted from the porphyrjn a obtained by our method, with haemin a isolated directly without removal of iron by other workers (Warburg and Gcwitz, 1051;Kiese and Kurz, 1954).…”

mentioning

confidence: 97%

Porphyrins With Formyl Groups Vi

Lemberg

Stewart

1955

Aust J Exp Biol Med

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“…Mitochondria of all cells contained cytochrome c (549 nm). &heme s87nm a = 27.4 mM-' x cm-' [18], &hemea -5s7nm -8.4 mM-' x cm-' [19], Mitochondria1 Pvotein Synthesis &protoheme 587nm --1.3 mM-'xcm-' [20], in Cytochrome-Oxidase-Deficient Cells…”

Section: Immunological Proceduresmentioning

confidence: 99%

Precursors of Cytochrome Oxidase in Cytochrome‐Oxidase‐Deficient Cells of Neurospora crassa

Werner

Schwab

Neupert

1974

European Journal of Biochemistry

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Three different cell types of Neurospora crassa deficient in cytochrome oxidase were studied: the nuclear mutant cni‐1, the cytoplasmic mutant mi‐1 and copper‐depleted wild‐type cells. The enzyme‐deficient cells have retained a functioning mitochondrial protein synthesis. It accounted for 12–16% of the total protein synthesis of the cell. However, the analysis of mitochondrial translation products by gel electrophoresis revealed that different amounts of individual membrane proteins were synthesized. Especially mutant cni‐1 produced large amounts of a small molecular weight translation product, which is barely detectable in wild‐type. Mitochondrial preparations of cytochrome‐oxidase‐deficient cells were examined for precursors of cytochrome oxidase. The presence of polypeptide components of cytochrome oxidase in the mitochondria was established with specific antibodies. On the other hand, no significant amounts of heme a could be extracted. Radioactively labelled components of cytochrome oxidase were isolated by immunoprecipitation and analysed by gel electrophoresis. All three cell types contained the enzyme components 4–7, which are translated on cytoplasmic ribosomes. The mitochondrially synthesized components 1–3 were present in mi‐1 mutant and in copper‐depleted wild‐type cells. In contrast, components 2 and 3 were not detectable in the nuclear mutant cni‐1. Both relative and absolute amounts of these polypeptides in the enzyme‐deficient cells were quite different from those in wild‐type cells. The components of cytochrome oxidase found in the enzyme‐deficient cells were tightly associated with the mitochondrial membranes. Processes, which affect and may control the production of enzyme precursors or their assembly to a functional cytochrome oxidase are discussed.

show abstract

H�moglobine und andere H�moproteine

Cited by 6 publications

References 102 publications

Porphyrins With Formyl Groups V

Porphyrins With Formyl Groups V

Porphyrins With Formyl Groups Vi

Precursors of Cytochrome Oxidase in Cytochrome‐Oxidase‐Deficient Cells of Neurospora crassa

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