scholarly journals Role of avidin and other biotin-binding proteins in the deposition and distribution of biotin in chicken eggs. Discovery of a new biotin-binding protein

1987 ◽  
Vol 241 (3) ◽  
pp. 677-684 ◽  
Author(s):  
H B White ◽  
C C Whitehead

In addition to the previously characterized egg-yolk biotin-binding protein (BBP-I), we have discovered another BBP (BBP-II) in the plasma and yolk from laying hens. BBP-I is stable to 65 degrees C, whereas BBP-II is stable to 45 degrees C. Both proteins are normally saturated with biotin and together they account for most, if not all, of the biotin in hen plasma and yolk, except in hens fed excessive amounts of biotin (greater than 1 mg of biotin/kg of feed). The maximal production of BBP-I is attained at lower levels of dietary biotin (approximately 50 micrograms/kg) than for BBP-II (approximately 250 micrograms/kg); however, the maximal production of BBP-II is severalfold greater than for BBP-I. Consequently, as dietary biotin increases, the ratio of BBP-II to BBP-I increases and becomes constant at dietary intakes of biotin above 250 micrograms/kg. The observation that the amounts of these proteins are limited by biotin in the normal dietary range (less than 250 micrograms/kg) suggests that biotin is required for the synthesis, secretion or stability of these proteins. Although both plasma vitamin-protein complexes are transported to the oocyte and concentrated in the yolk, BBP-II is transferred more efficiently. Thus biotin deposition in the yolk is a function of the amounts and relative concentrations of the two proteins. Dietary biotin above 250 micrograms/kg exceeds the transport capacity of BBP-I and BBP-II in the plasma; however, unbound biotin does not accumulate. Rather it is efficiently scavenged by avidin in the oviduct and transferred to the egg albumen. Only when avidin becomes saturated at high dietary intake does free or weakly bound biotin accumulate in plasma and yolk. The synthesis of avidin is independent of dietary biotin. Small amounts of BBPs with the heat-stability of avidin or BBP-I respectively are present in the plasma of adult males or immature chickens. BBP-II, the major BBP in the plasma and yolk of laying hens, was not detected in the plasma of non-laying chickens.

1976 ◽  
Vol 157 (2) ◽  
pp. 395-400 ◽  
Author(s):  
H B White ◽  
B A Dennison ◽  
M A Della Fera ◽  
C J Whitney ◽  
J C McGuire ◽  
...  

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.


1978 ◽  
Vol 175 (2) ◽  
pp. 629-633 ◽  
Author(s):  
R D Mandella ◽  
H W Meslar ◽  
H B White

The plasma of laying hens contains a specific biotin-binding protein that appears to be identical with an egg-yolk biotin-binding protein. Both proteins are saturated with biotin and require elevated temperatures to effect the exchange of [14C]biotin for the protein-bound vitamin. The heat-exchange curve in each case is the same and differs sharply from that of avidin, the egg-white biotin-binding protein. On Sephadex G-100 gel filtration, plasma and yolk biotin-binding proteins were each eluted slightly ahead of avidin (mol.wt. 68,000), suggesting that they are of similar molecular weight. Plasma and yolk biotin-binding proteins required the same ionic strength to be eluted from a phosphocellulose ion-exchange column. Both the plasma and yolk biotin-binding proteins had a pI of 5; avidin has a pI of 10. Plasma biotin-binding protein cross-reacted with antiserum to yolk biotin-binding protein and showed a precipitin line of identity with purified yolk biotin-binding protein. It is suggested that biotin-binding plays an important role in mediating the transport of the vitamin from the bloodstream to the developing oocyte.


1978 ◽  
Vol 253 (19) ◽  
pp. 6979-6982 ◽  
Author(s):  
H.W. Meslar ◽  
S.A. Camper ◽  
H.B. White

2020 ◽  
Vol 98 (Supplement_4) ◽  
pp. 252-253
Author(s):  
Cherrie Nolden ◽  
Abbey Grisham ◽  
Dan Schaefer ◽  
Matt Akins ◽  
Mark Cook

Abstract Antibody production in egg yolks of immunized laying hens is an alternative to conventional mammalian production. Antibody yield peak and duration have not been described for immunoglobulin Y technology using Freund’s incomplete adjuvant (FIA) and C-phosphate-guanosine oligodeoxynucleotides (CpG-ODN) without the inclusion of Freund’s complete adjuvant for enhancing the immune response to an interleukin-10 (IL-10) peptide. This study sought to describe the antibody titer production for an 8 amino acid sequence from the surface of the bovine IL-10 protein (VMPQAENG) as the antigen emulsified with CpG-ODN and FIA in phosphate buffered saline (PBS). 60 hens were assigned to receive the complete vaccine (Peptide), 20 received the vaccine without the IL-10 peptide (Control), and 8 received a PBS injection (Blank). Hens were immunized with 0.25 mL in 4 locations, each breast and each thigh on days 1, 15 and 29. The complete vaccine delivered 0.6 mg IL-10 peptide, 8 µg CpG-ODN, and 0.33 mL FIA per hen on each vaccination day. Eggs were collected regularly until 175 days after the first immunization and the anti IL-10 peptide activities of the yolk were determined by ELISA. Egg titers by treatment were analyzed with a repeated measures ANOVA in SAS. The supplementation of FIA with CpG-ODN produced high titers, of over 100 µg of antibody per mL of yolk (µg Ab/mL yolk), around day 33 through day 76, with a slow decline through day 175 when average titers remained above 40 µg Ab/mL yolk. Peptide egg titers were significantly higher than Blank or Control titers from day 31 though day 175 (P < 0.0001). Titers recovered from Marcq et al. (2015) with similar methods were 1.5 to 7 times lower than these results over the same number of days.


Author(s):  
Y. Martínez ◽  
C.E. Orozco ◽  
R.M. Montellano ◽  
M. Valdivié ◽  
C.A. Parrado
Keyword(s):  
Egg Yolk ◽  

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