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Availability of avidin-bound biotin to the chicken embryo

Authors
Journal
Archives of Biochemistry and Biophysics
0003-9861
Publisher
Elsevier
Publication Date
Volume
298
Issue
1
Identifiers
DOI: 10.1016/0003-9861(92)90096-f
Keywords
  • Enzyme Structure And Mechanisms
  • Cellular Regulation
  • Phosphorylation And Dephosphorylation
Disciplines
  • Biology

Abstract

Abstract Avidin, an exceptionally stable protein in egg white, binds the vitamin biotin with very high affinity and can induce biotin deficiency when fed to animals. To determine if biotin bound to avidin is available to the chicken embryo, the fate of [ 3H]biotin complexed to avidin was monitored during embryonic development. The majority (>85%) of the [ 3H]biotin was extraembryonic until the day before hatching, when embryos swallow egg white and withdraw the yolk sac into their abdomen. Thus, biotin in the egg white of chicken eggs contributes little to the biotin status of the chick prior to hatching. After hatching, much of the [ 3H]biotin was assimilated. About 30% of the total was found in the liver and kidneys by 4 days of age. The biotin in liver was associated with large proteins and not with avidin. In a separate experiment, biotin injected into the egg white of biotin-deficient eggs failed to increase embryonic development or hatchability. Both experiments suggest that biotin in egg yolk is the primary and virtually sole source of biotin for the chicken embryo.

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