The nature of the biochemical lesion in avian renal riboflavinuria III. The isolation and characterization of the riboflavin-binding protein from egg albumen

Farrell, Harold M.; Mallette, M. F.; Buss, E. G.; Clagett, C. O.

doi:10.1016/0005-2795(69)90103-2

Cited by 71 publications

(19 citation statements)

References 20 publications

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“…The standard RBP used in the immuno plate assay was isolated as described by Farrell et al (1969). RBP rabbit antiserum was prepared by the method of Farrell et al (1970a).…”

Section: Separation Of Individual Egg Partsmentioning

confidence: 99%

Avian Riboflavinuria

1975

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The riboflavin binding protein (RBP) content of individual egg components were followed through the development of fertilized eggs. Total proteins of the tissues were analyzed. The disappearance of RBP from the yolk and albumen occurred at the same rate as the total proteins. There was no evidence of any increase of free riboflavin nor degraded RBP in the yolk and albumen. Hence, it appears that the riboflavin was taken in by the embryo as the riboflavin-protein complex. The individual embryos showed some RBP accumulation through the first fourteen days of development. This may be an indication that the embryo is taking in the riboflavin-protein complex faster than riboflavin is utilized during the early stages of incubation. However, the beginning of a more rapid rate of growth at 13-14 days, was associated with the start of a gradual decline in the level of RBP in the embryo. This may suggest that the need for riboflavin exceeds the rate of transfer from the yolk and albumen reservoirs. RBP-riboflavin complex appears to be degraded after transfer to the embryo.

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“…The standard RBP used in the immuno plate assay was isolated as described by Farrell et al (1969). RBP rabbit antiserum was prepared by the method of Farrell et al (1970a).…”

Section: Separation Of Individual Egg Partsmentioning

confidence: 99%

Avian Riboflavinuria

1975

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“…The respective dependence of the chemical shifts ( fig.4) indicates the only distinct upfield shift for H(9), slight down~eld shift for H (6), and the tendency toward the separation of the ~bo~a~ peaks with decreasing riboflavin ,: apoprotein molar ratio for both aryl protons and to a lesser extent for methyl groups.…”

Section: Resultsmentioning

confidence: 96%

Proton NMR study of the interaction of riboflavin with the egg‐yolk apoprotein

Lubas

Sołtysik

Steczko³

et al. 1977

FEBS Letters

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“…Pig kidney general acyl-CoA dehydrogenase was obtained as described previously (Thorpe, 1981), electron transferring flavoprotein was a gift from Mr. Robert Gorelick, University of Delaware (Gorelick et al, 1982), and egg white riboflavinbinding protein (Farrell et al, 1969) The buffer used throughout this work was 50mM-potassium phosphate, pH 7.6, containing 0.3mM-EDTA. Flavoprotein concentrations were determined with the following absorption coefficients for bound flavin: acyl-CoA dehydrogenase, 15.4mM--cm-I at 446nm ; electron transferring flavoprotein, 13.3 mm-1 cm-at 436nm (Gorelick et al, 1982); and egg white riboflavin-binding protein, 11mM-m lcm-I at 455nm (Kosik, 1982).…”

Section: Methodsmentioning

confidence: 99%

The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other flavoproteins

Madden¹,

Lau²,

Thorpe³

1984

Biochemical Journal

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Pig kidney general acyl-CoA dehydrogenase is markedly stabilized against loss of flavin and activity in 7.3M-urea or at 60°C upon reduction with sodium dithionite or octanoyl-CoA. Electron transferring flavoprotein is similarly stabilized, whereas egg white riboflavin-binding protein loses flavin more readily on reduction. These and other data support the anticipated correlation between the kinetic stability of the holoproteins and the oxidation-reduction potential of their bound flavins.

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The nature of the biochemical lesion in avian renal riboflavinuria III. The isolation and characterization of the riboflavin-binding protein from egg albumen

Cited by 71 publications

References 20 publications

Avian Riboflavinuria

Avian Riboflavinuria

Proton NMR study of the interaction of riboflavin with the egg‐yolk apoprotein

The influence of oxidation-reduction state on the kinetic stability of pig kidney general acyl-CoA dehydrogenase and other flavoproteins

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