1975
DOI: 10.3382/ps.0540562
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Avian Riboflavinuria

Abstract: 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 … Show more

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Cited by 7 publications
(2 citation statements)
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“…Riboflavin-binding protein, synthesized by the chicken liver in response to estrogen, 58 is secreted into the blood and transferred to the growing follicles. 59 The accumulation of riboflavin in embryo tissues on E14 coincides with the riboflavin-binding protein disappearance from the egg yolk and egg white compartments, 60 consistent with the observation of a decreased relative abundance observed in egg yolk after E12. 57 The alterations of egg yolk proteome at different times (E0, E7, E14, and E18) were analyzed to further study the dynamics of egg yolk proteins during the entire period.…”
Section: ■ Egg Omics During Embryonic Developmentsupporting
confidence: 78%
“…Riboflavin-binding protein, synthesized by the chicken liver in response to estrogen, 58 is secreted into the blood and transferred to the growing follicles. 59 The accumulation of riboflavin in embryo tissues on E14 coincides with the riboflavin-binding protein disappearance from the egg yolk and egg white compartments, 60 consistent with the observation of a decreased relative abundance observed in egg yolk after E12. 57 The alterations of egg yolk proteome at different times (E0, E7, E14, and E18) were analyzed to further study the dynamics of egg yolk proteins during the entire period.…”
Section: ■ Egg Omics During Embryonic Developmentsupporting
confidence: 78%
“…[8,9] While plausible, it is still not clear how halobacterial dodecins actually switch between storage and release, since the dodecin of H. salinarum (HsDod) is constantly present in the cell, [7] whereas the avian RbF binding protein is degraded after a certain time during the embryonal development in the egg. [10][11][12] The dodecin protein family is not limited to archaea and dodecin encoding genes are ubiquitous spread among the different Phyla of bacteria. Despite this, so far, only the bacterial dodecins of Halorhodospira halophila (H. halophila; HhDod) [5,7] , Thermus thermophilus (T.…”
mentioning
confidence: 99%