The studies reported here indicate that tanned red cells coated with a mixture of chromatographically purified ovalbumin and conalbumin give agglutination titres which are directly related to the amount of antibody (as measured by quantitative precipitation) present against either of these antigens in mixed sera. With whole (unabsorbed) mixed sera, these coated cells record the titre of the major antibody present, whether this is anti-ovalbumin or anti-conalbumin. There was no evidence of greater sensitivity to anti-conalbumin. A trace of ovalbumin in a preparation of conalbumin used to coat cells is fully sufficient to enable them to react with any anti-ovalbumin in a serum. Twice recrystallized ovalbumin still contains some conalbumin. Sera raised against it may contain unexpectedly high levels of anti-conalbumin and this could cause confusion in tanned red cell tests.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1409188 | PMC |
Food Chem
May 2023
Ph.D. Program in Nutrition and Food Science, Fu Jen Catholic University, New Taipei City 242, Taiwan; Department of Food Science, Fu Jen Catholic University, New Taipei City 242, Taiwan. Electronic address:
The effects of transglutaminase (TGase, 1.0 unit/mL) with heat (95 °C, 5 min), 2-mercaptoethanol (2-ME, 0.83 %), and l-cysteine (l-Cys, 50 mM) pretreatment on the cross-linking of ovalbumin (OVA) and ovotransferrin (OVT) were investigated.
View Article and Find Full Text PDFFood Chem
March 2023
Department of Food Science and Technology, University of Nebraska-Lincoln, Lincoln, NE 68588-6205, United States. Electronic address:
Radiofrequency (RF) assisted thermal processing can significantly enhance the gel firmness of egg white powder compared to the traditional hot room (HR) processing. Thus, the present study aims to delineate the impact of RF processing on the proteins' structure and bio-functional properties of egg white protein gels. The secondary protein conformations of egg white proteins exhibited no significant alteration upon RF-assisted thermal processing over traditional HR processing.
View Article and Find Full Text PDFFood Chem
March 2023
Department of Nutritional Sciences, University of Connecticut, Storrs, CT 06269, USA. Electronic address:
Egg proteins, as one of the most abundant animal protein sources, have received considerable attention for developing delivery systems. Among all egg proteins, egg white (ovalbumin) is the most promising encapsulant due to its excellent properties such as gelling, digestibility, self-assembly, amphiphilic nature. In this review paper, we focused particularly on egg protein-based delivery systems with superior encapsulation and delivery functions, including polymeric nanoparticles, emulsions, hydrogels and aerogels.
View Article and Find Full Text PDFFood Chem
January 2022
Meat Processing Key Laboratory of Sichuan Province, School of Food and Biological Engineering, Chengdu University, Chengdu 610106, China. Electronic address:
Clarification of the mechanism of heat-induced gel formation by proteins under natural food systems could provide important references for the regulation of food texture. In the present study, the proteins involved in the early stage (heating at 72 °C for 8 min) of egg-white thermal gel (EWG) formation were studied quantitatively through comparative proteomic analysis. We discovered that the abundance of ovalbumin and ovomucoid increased significantly (p < 0.
View Article and Find Full Text PDFJ Sep Sci
September 2021
CAS Key Laboratory of Soft Matter Chemistry, Department of Polymer Science and Engineering, University of Science and Technology of China, Hefei, P. R. China.
A mixed polymer brushes material based on poly (2-methyl-2-oxazoline)- and poly (acrylic acid)-coated capillary with switchable protein adsorption/desorption properties was applied for online preconcentration of lysozyme in hen egg white during capillary electrophoresis performance. First, lysozyme in simulated egg white was successfully online preconcentrated and the detection signal of lysozyme was amplified. Ovalbumin, ovomucoid, and conalbumin in egg white were verified show negligible interference on the online preconcentration of lysozyme according to the study on electroosmotic flow mobility.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!