Effect of Vitamin D3 on Mitochondrial Membrane of Rat Liver

Abe, Takashi; Muto, Yasutoshi; Hosoya, Norimasa

doi:10.5925/jnsv1954.17.185

Cited by 4 publications

(5 citation statements)

References 9 publications

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“…Thus, considerable purification was achieved using preparative polyacrylamide gel electrophoresis under non-denaturing conditions. Gel permeation chromatography, using a Superose-12 column, indicated an apparent molecular mass of 56.4 kDa, agreeing with previous estimates of the molecular mass of the native protein [61]. Upon electrophoresis in SDSIPAGE, the protein dissociated into subunits of mass 15 kDa, agreeing with previous estimates by others [61] and confirming that chicken transthyretin, like mammalian transthyretins, is a tetramer.…”

Section: Isolation Of Chicken Transthyretinsupporting

confidence: 81%

“…Gel permeation chromatography, using a Superose-12 column, indicated an apparent molecular mass of 56.4 kDa, agreeing with previous estimates of the molecular mass of the native protein [61]. Upon electrophoresis in SDSIPAGE, the protein dissociated into subunits of mass 15 kDa, agreeing with previous estimates by others [61] and confirming that chicken transthyretin, like mammalian transthyretins, is a tetramer. Further evidence for the identity of the purified protein was obtained by demonstration that the protein bound [ '251]thyroxine and migrated with the same electrophoretic mobility under non-denaturing conditions at pH 8.6 as the complex of thyroxine and transthyretin from serum.…”

Section: Isolation Of Chicken Transthyretinsupporting

confidence: 81%

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Isolation, characterization, cDNA cloning and gene expression of an avian transthyretin

Duan

Achen

Richardson

et al. 1991

European Journal of Biochemistry

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A chicken liver cDNA library was constructed in bacteriophage AgtlO. A full-length transthyretin cDNA clone was identified by screening with rat transthyretin cDNA and was sequenced. A three-dimensional model of chicken transthyretin was obtained by computer-graphics-based prediction from the derived amino acid sequence for chicken transthyretin and from the structure of human transthyretin determined by X-ray diffraction analysis

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Section: Isolation Of Chicken Transthyretinsupporting

confidence: 81%

Section: Isolation Of Chicken Transthyretinsupporting

confidence: 81%

Isolation, characterization, cDNA cloning and gene expression of an avian transthyretin

Duan

Achen

Richardson

et al. 1991

European Journal of Biochemistry

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“…The defect in these chickens is the lack of a functional riboflavin-binding protein (Winter et al, 1967a). These results in particular and the similarity of this system to transferrin, retinolbinding protein (Abe et al, 1975) and vitamin B-12binding protein (Sonneborn & Hansen, 1970) in chickens suggest that vitamin and mineral transport should be viewed as a problem ofprotein transport.…”

mentioning

confidence: 83%

Biotin-binding protein from chicken egg yolk. Assay and relationship to egg-white avidin

White¹,

Dennison²,

Fera³

et al. 1976

Biochemical Journal

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1. Biotin in chicken egg yolk is non-covalently bound to a specific protein that comprises 0.03% of the total yolk protein (0.8 mg/yolk). This biotin-binding protein is not detectable by the normal avidin assay owing to the biotin being tightly bound. Exchange of [14C]biotin for bound biotin at 65 degrees C is the basis of an assay for this protein. 2. Biotin-binding protein from egg yolk is distinguishable from egg-white avidin on Sephadex G-100 gel filtration, although the sizes of the two proteins appear quite similar. 3. Biotin-binding protein is denatured at a lower temperature and freely exchanges biotin at lower temperatures than does avidin. 4. The biotin-binding protein in egg yolk is postulated to be responsible for the deposition of biotin in egg yolk. D-[carboxyl-14C]Biotin injected into laying hens rapidly appears in the egg bound to yolk biotin-binding protein and avidin. Over 60% of the radioactivity is eventually deposited in eggs. The kinetics of biotin deposition in the egg suggests a 25 day half-life for an intracellular biotinyl-coenzyme pool in the laying hen.

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“…The mode of deposition in adequate amounts of some of the vitamins and other micronutrients in the chicken egg for the 21-day development of the prospective embryo involves the participation of carrier proteins specific for each of these nutrients. This is exemplified by the discovery in recent years of the binding proteins for biotin (Eakin et al, 1940;White et al, 1976), riboflavin (Rhodes et al, 1959;Murthy & Adiga, 1977), vitamin B12 (Sonneborn & Hensen, 1970), retinol (Abe et al, 1975) and cholecalciferol (Fraser & Emtage, 1976). An intriguing aspect of these proteins is the higher specificity and avidity of their interaction with the free vitamins than with the respective active metabolites/coenzyme forms.…”

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confidence: 99%

Isolation and characterization of thiamin-binding protein from chicken egg white

Muniyappa¹,

Adiga²

1979

Biochemical Journal

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A thiamin-binding protein was isolated and characterized from chicken egg white by affinity chromatography on thiamin pyrophosphate coupled to aminoethyl-Sepharose. The high specificity of interaction between the thiamin-binding protein and the riboflavin-binding protein of the egg white, with a protein/protein molar ratio of 1.0, led to the development of an alternative procedure that used the riboflavin-binding protein immobilized on CNBr-activated Sepharose as the affinity matrix. The thiamin-binding protein thus isolated was homogeneous by the criteria of polyacrylamide-gel disc electrophoresis, double immunodiffusion and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, had a mol.wt. of 38,000 +/- 2000 and was not a glycoprotein. The protein bound [14C]thiamin was a molar ratio of 1.0, with dissociation constant (Kd) 0.3 micrometer.

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Effect of Vitamin D3 on Mitochondrial Membrane of Rat Liver

Cited by 4 publications

References 9 publications

Isolation, characterization, cDNA cloning and gene expression of an avian transthyretin

Isolation, characterization, cDNA cloning and gene expression of an avian transthyretin

Biotin-binding protein from chicken egg yolk. Assay and relationship to egg-white avidin

Isolation and characterization of thiamin-binding protein from chicken egg white

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