Site of Egg White Protein Formation

Mandeles, Stanley; Ducay, Eufemio D.

doi:10.1016/s0021-9258(18)50143-5

Cited by 50 publications

(2 citation statements)

References 11 publications

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“…The proteins can be purified from egg white (Rhodes et al ., 1959), egg yolk (Ostrowski et al ., 1962) and from the plasma of laying hens (Miller et al ., 1982a). Egg white RfBP is synthesized by the oviduct cells (Mandeles and Ducay, 1962), plasma RfBP is produced in the liver under estrogen control and yolk RfBP is the result of a proteolytic cleavage of the last 11‐13 amino acids of plasma RfBP when the molecule crosses the oocyte membrane (Norioka et al ., 1985). The three proteins have a single binding site for riboflavin with a dissociation constant of 1.3 nM in the pH range 6‐9; removal of the vitamin from the holoprotein is accomplished at lower pH where the affinity for the specific ligand is substantially reduced (Müller and van Berkel, 1991).…”

Section: Introductionmentioning

confidence: 99%

Crystal structure of chicken riboflavin-binding protein

1997

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play an essential role in the survival of the fetus.The family of the chicken RfBPs includes three wellThe crystal structure of chicken egg white riboflavinknown proteins that are the product of the same gene but binding protein, determined to a resolution of 2.5 Å, have undergone different post-translational modifications is the prototype of a family that includes other ribo- (White and Merrill, 1988). The proteins can be purified flavin-and folate-binding proteins. An unusual characfrom egg white (Rhodes et al., 1959), egg yolk (Ostrowski teristic of these molecules is their high degree of cross et al., 1962) and from the plasma of laying hens (Miller linking by disulfide bridges and, in the case of the et al., 1982a). Egg white RfBP is synthesized by the avian proteins, the presence of stretches of highly oviduct cells (Mandeles and Ducay, 1962), plasma RfBP phosphorylated polypeptide chain. The structure of is produced in the liver under estrogen control and yolk chicken egg white riboflavin-binding protein is characRfBP is the result of a proteolytic cleavage of the last terized by a ligand-binding domain and a phosphoryl-11-13 amino acids of plasma RfBP when the molecule ated motif. The ligand-binding domain has a fold that crosses the oocyte membrane (Norioka et al., 1985). The appears to be strongly conditioned by the presence three proteins have a single binding site for riboflavin of the disulfide bridges. The phosphorylated motif, with a dissociation constant of 1.3 nM in the pH range essential for vitamin uptake, is made up of two helices 6-9; removal of the vitamin from the holoprotein is found before and after the flexible phosphorylated accomplished at lower pH where the affinity for the region. The riboflavin molecule binds to the protein specific ligand is substantially reduced (Müller and van with the isoalloxazine ring stacked in between the rings Berkel, 1991

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Section: Introductionmentioning

confidence: 99%

Crystal structure of chicken riboflavin-binding protein

1997

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“…white is synthesized in the oviduct (Mandeles & Ducay, 1962). A mutant strain of chickens unable to synthesize RBP is also unable to deposit adequate amounts of riboflavin in its eggs even when given large amounts of the vitamin (Maw, 1954;Boucher et al, 1964;Winter et al, 1967).…”

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Highly phosphorylated region of chicken riboflavin-binding protein: chemical characterization and phosphorus-31 NMR studies

Miller¹,

Mas²,

White³

1984

Biochemistry

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Phosphate residues on chicken riboflavin-binding protein (RBP) have been implicated in the recognition and deposition of the protein-vitamin complex in egg yolk by the ovary. We demonstrate that all of the phosphate of RBP is linked to serine and that most if not all of the phosphoserine residues are contained in a single tryptic peptide having a composition SerP8, Glx6, His2, Leu2, Ala, Met, Lys. Despite differences in the tissue of synthesis, RBPs isolated from egg yolk and egg white yield phosphopeptides virtually identical in their amino acid composition and 101-MHz 31P NMR spectra. This implies that posttranslational phosphorylation of RBP is the same in liver and oviduct. The 31P NMR spectrum of the phosphopeptide is quite different from that of the phosphoprotein. The 31P NMR spectra of egg yolk and egg white RBP are quite similar but not identical and are unaffected by the binding of riboflavin. Optimal resolution of seven phosphorus resonances was obtained near pH 7.0. The titration behavior of all the phosphoserine residues is similar. We propose that this highly anionic peptide, exposed at the surface of RBP, is the principal determinant for the uptake of RBP by the vitelline membrane of the ovarian follicle.

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Oviductal morphology and eggshell formation in the lizard, Sceloporus woodi

Palmer

DeMarco

Guillette

1993

Journal of Morphology

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Despite a great deal of work in recent years on the structure of reptilian eggshells, few studies have examined the structure and regulation of the female reproductive tract in the formation of eggshell components, and none have examined the entire process from ovulation to oviposition. In this study, we examined oviductal structure in the oviparous lizard, Sceloporus woodi, followed changes in oviductal structure during gravidity, and determined uterine function in the formation of eggshell components. The endometrial glands of the uterus produce the proteinaceous fibers of the eggshell membrane mainly during the first 24 hours following ovulation, and the fibers are secreted intact and subsequently wrapped around the in utero eggs. Eggshell fibers of different thicknesses are layered around each egg, ranging from an inner layer of thick fibers that gradually become thinner medially and finally forms an outer layer of densely packed particulate matter. These changes in the fibrous layer are reflected by the thickness and length of fibers released from the endometrial glands. Calcium deposition occurs from 3 days following ovulation through day 14 (oviposition) and is accompanied by cellular changes in the luminal epithelium suggestive of secretory activity. Deposition of the eggshell components within the uterus occurs on all eggs simultaneously, rather than sequentially. © 1993 Wiley-Liss, Inc.

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Site of Egg White Protein Formation

Cited by 50 publications

References 11 publications

Crystal structure of chicken riboflavin-binding protein

Crystal structure of chicken riboflavin-binding protein

Highly phosphorylated region of chicken riboflavin-binding protein: chemical characterization and phosphorus-31 NMR studies

Oviductal morphology and eggshell formation in the lizard, Sceloporus woodi

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