The Flavoprotein-Apoprotein System of Egg White

Rhodes, Marvin B.; Bennett, N. B.; Feeney, Robert E.

doi:10.1016/s0021-9258(18)69866-7

Cited by 153 publications

(24 citation statements)

References 17 publications

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“…Spectral analysis showed absorption maxima at 275 and 442 nm. These results indicate the presence of riboflavin as well as the flavoprotein system of the egg albumen (Rhodes et al, 1959).…”

Section: Resultsmentioning

confidence: 60%

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Characterization of the exudate from cooked shell eggs

Nath¹,

Vadehra²,

Baker³

1972

J. Agric. Food Chem.

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Boiled and peeled eggs stored in Cryovac bags at 5°C produced a greenish-yellow fluorescent exudate.The amount of exudate increased from 1.26% at 1 day to 2.7% at 7 days, with no further increase on storage. The freeze-dried exudate contained 61 % protein, 21.25% carbohydrate, and 8.9% minerals.Chromatography of the exudate on Sephadex G-50 produced five fractions. The first two fractions, based on biological activity and chemical analysis, appeared to be ovomucoid-like. Fractions 3 and 4 contained large amounts of carbohydrate but their exact nature could not be established. Fraction 5 was fluorescent and appeared to be a component of the flavoprotein moiety in albumen.

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“…Spectral analysis showed absorption maxima at 275 and 442 nm. These results indicate the presence of riboflavin as well as the flavoprotein system of the egg albumen (Rhodes et al, 1959).…”

Section: Resultsmentioning

confidence: 60%

“…Pure riboflavin absorbs maximally at 445 nm, and the absorption is quenched by the addition of sodium hydrosulfite (Rhodes et al, 1959). The peak at 442 nm in the exudate may be due to the presence of riboflavin, and this was further indicated by the addition of sodium hydrosulfite (Figure 2).…”

Section: Resultsmentioning

confidence: 96%

Characterization of the exudate from cooked shell eggs

Nath¹,

Vadehra²,

Baker³

1972

J. Agric. Food Chem.

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“…Riboflavin binding protein (RBP) was prepared from egg white as apoprotein and reconstituted by adding riboflavin according to the method by Rhodes et al 7 Glucose oxidase from Aspergillus niger (GOD) was purchased from Nacalai Tesque (Kyoto, Japan) and purified according to Tsuge et al 8 Buffer solution of flavoprotein sample was made to flow through a 1 mm cell, and a femtosecond up-conversion apparatus for the measurement of fluorescence dynamics was similar to that described elsewhere. 9 The fwhm of the instrumental response was 210 fs.…”

Section: Methodsmentioning

confidence: 99%

“…Riboflavin binding protein (RBP) was prepared from egg white as apoprotein and reconstituted by adding riboflavin according to the method by Rhodes et al Glucose oxidase from Aspergillus niger (GOD) was purchased from Nacalai Tesque (Kyoto, Japan) and purified according to Tsuge et al…”

Section: Methodsmentioning

confidence: 99%

Ultrafast Fluorescence Quenching Dynamics of Flavin Chromophores in Protein Nanospace

et al. 1998

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We have studied excited-state dynamics of “nonfluorescent” flavoproteins by means of the femtosecond fluorescence up-conversion method. We have interpreted the ultrafast fluorescence quenching mechanisms of these flavoproteins as due to the ultrafast electron transfer or electron transfer followed by proton-transfer interactions between excited flavin chromophore and nearby tryptophan and tyrosine residues placed in the protein nanospace, on the basis of their X-ray structures. Comparisons of fluorescence time profiles and spectral characteristics of flavin chromophores in solutions with those in protein environments have suggested the existence of extremely fast Franck−Condon → fluorescent state relaxations specific to the protein environments. These results of the ultrafast fluorescence dynamics studies on the nonfluorescent flavoproteins have many features in common with other photobiologically important proteins.

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“…The demineralized particles were partially dephosphorylated by treatment with potato acid phosphatase as described by Rhodes et al (1959); 0.8 mL of phosphatase (60 units/mL) was added to 35 mL of demineralized particles (5.0 pmol of organic phosphate/mL) and dialyzed overnight against 600 mL of 0.1 M sodium acetate, pH 5.3 at 37 °C. Only 25% of the organic phosphate was liberated, and addition of more enzyme did not liberate a significant amount of additional 1 Abbreviations: EDTA, ethylenediaminetetraacetic acid; Tris, tris-(hydroxymethyl)aminomethane.…”

Section: Methodsmentioning

confidence: 99%

Phosphoprotein particles: calcium and inorganic phosphate binding structures

Marsh¹,

Sass²

1984

Biochemistry

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Phosphoprotein particles were isolated in their native state from the physiological fluid of the estuarine clam Rangia cuneata , and the characteristics of the mineral ion-protein complex which constitutes the native particle were investigated by using mineral ion binding and mineral ion exchange techniques. The particles are aspartic acid rich, highly phosphorylated proteins containing calcium, magnesium, and inorganic phosphate ions and covalently cross-linked via histidinoalanine residues. Twenty-nine percent of the amino acid residues are phosphorylated. In their native state, the particles contain a protected pool of calcium and inorganic phosphate ions and an exchangeable pool of calcium and magnesium ions. The Ca/PO4 ratio in the protected pool is about 2.5. The number of binding sites for the protected mineral is unknown, but on the average, the native particles contain about 0.2 inorganic phosphate ion per organic phosphate residue. There is 1.0 exchangeable metal ion binding site per organic phosphate residue, and there is probably a phosphoserine residue at each site. These sites bind calcium with an apparent binding constant (KCa) of 4 X 10(3) M-1 at 50% saturation under physiological conditions, and KCa/ KMg is about 1.6. In vivo, about 85% of the exchangeable sites are occupied. The total number of calcium ion binding sites (N) in the phosphoprotein particles is related to the number of organic phosphate residues (Po) and the number of bound inorganic phosphate ions (Pi) by the equation N = Po + 2. 5Pi . The phosphoprotein particles probably serve as both the transporter and reserve source of calcium ions for shell development.

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The Flavoprotein-Apoprotein System of Egg White

Cited by 153 publications

References 17 publications

Characterization of the exudate from cooked shell eggs

Characterization of the exudate from cooked shell eggs

Ultrafast Fluorescence Quenching Dynamics of Flavin Chromophores in Protein Nanospace

Phosphoprotein particles: calcium and inorganic phosphate binding structures

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