The transcription of structural and intervening sequences of the chicken ovalbumin gene was studied in nuclei isolated from the oviduct, liver, and spleen of chickens in different states of estrogen simulation. The concentration of transcripts of structural and intervening DNA sequences was determined by hybridizing the newly synthesized [(3)H]RNA to filters containing cloned ovalbumin cDNA (pO...

Polysomes involved in ovalbumin synthesis were identified by the binding of 1251-anti-ovalbumin to hen oviduct polysomes. Techniques were developed for the isolation of undegraded hen oviduct polysomes and for the preparation of 1251-y-globulin free of ribonuclease activity. The distribution of 1251-anti-ovalbumin in the polysome profile is in accordance with the size of the polysomes that are ...

Food-derived bioactive peptides are promising ingredients for developing functional foods and nutraceuticals due to their putative safety, low cost, multiple health benefits. Chicken egg is considered a major source of dietary protein, lipids, vitamins, minerals but also highly allergenic. The aim this work was investigate the inherent properties chicken ovalbumin using in silico approaches. Ov...

Purified ovalbumin messenger RNA was employed to selectively enrich the concentration of the gene coding for ovalbumin from total chick DNA by molecular hybridization. The coding strand of the ovalbumin gene was partially purified from sheared chick DNA by affinity column chromatography using ovalbumin mRNA immobilized on phosphocellulose. The concentrations of the ovalbumin DNA sequence in var...

For the first time a comparative study on conformational differences between native ovalbumin and its heat-stable form, called S-ovalbumin, using small angle x-ray scattering, is reported. To detect a different pathway in the folding mechanism of the two proteins, scattering measurements have been performed on ovalbumin and S-ovalbumin denatured with different concentrations of guanidine hydroc...

Ovalbumin is partially homologous in sequence with the proteinase inhibitors alpha 1-proteinase inhibitor and anti-thrombin III. The region of sequence in ovalbumin which corresponds to the reactive sites of these proteinase inhibitors is susceptible to attack by subtilisin, elastase, thermolysin, bromelain, and Bacillus cereus protease. The esterase activity of elastase is not inhibited by ova...

A functional ovalbumin-dextran conjugate was prepared by dry-heated storage at 60 degrees C and 65% relative humidity for 3 weeks. The emulsifying properties of the ovalbumin-dextran conjugate were about three times higher than those of an ovalbumin-glucose conjugate. SDS-electrophoresis patterns showed that the ovalbumin-dextran conjugate obtained by dry-heating was not as polydispersed as tha...