Bovine plasma proteins increase virulence of Haemophilus somnus in mice

2007 ◽  
Vol 42 (1) ◽  
pp. 22-28 ◽  
Author(s):  
Roger S. Geertsema ◽  
Richard A. Kimball ◽  
Lynette B. Corbeil
Keyword(s):  
Plasma Proteins ◽  
Bovine Plasma ◽  
Haemophilus Somnus

scholarly journals Aggregation of Omic Data and Secretome Prediction Enable the Discovery of Candidate Plasma Biomarkers for Beef Tenderness

2020 ◽  
Vol 21 (2) ◽  
pp. 664 ◽  
Author(s):  
Sabrina Boudon ◽  
Joelle Henry-Berger ◽  
Isabelle Cassar-Malek
Keyword(s):  
Plasma Proteins ◽  
Biological Information ◽  
Plasma Proteome ◽  
Complex Phenotype ◽  
Beef Tenderness ◽  
Plasma Biomarkers ◽  
Bovine Plasma ◽  
Computational Reconstruction ◽  
Beef Sector ◽  
Omic Data

Beef quality is a complex phenotype that can be evaluated only after animal slaughtering. Previous research has investigated the potential of genetic markers or muscle-derived proteins to assess beef tenderness. Thus, the use of low-invasive biomarkers in living animals is an issue for the beef sector. We hypothesized that publicly available data may help us discovering candidate plasma biomarkers. Thanks to a review of the literature, we built a corpus of articles on beef tenderness. Following data collection, aggregation, and computational reconstruction of the muscle secretome, the putative plasma proteins were searched by comparison with a bovine plasma proteome atlas and submitted to mining of biological information. Of the 44 publications included in the study, 469 unique gene names were extracted for aggregation. Seventy-one proteins putatively released in the plasma were revealed. Among them 13 proteins were predicted to be secreted in plasma, 44 proteins as hypothetically secreted in plasma, and 14 additional candidate proteins were detected thanks to network analysis. Among these 71 proteins, 24 were included in tenderness quantitative trait loci. The in-silico workflow enabled the discovery of candidate plasma biomarkers for beef tenderness from reconstruction of the secretome, to be examined in the cattle plasma proteome.

Improvement of gluten-free bread properties by the incorporation of bovine plasma proteins and different saccharides into the matrix

2015 ◽  
Vol 170 ◽  
pp. 257-264 ◽  
Author(s):  
Laura T. Rodriguez Furlán ◽  
Antonio Pérez Padilla ◽  
Mercedes E. Campderrós
Keyword(s):  
Plasma Proteins ◽  
Gluten Free ◽  
Bovine Plasma ◽  
The Matrix ◽  
Bread Properties

Inulin like lyoprotectant of bovine plasma proteins concentrated by ultrafiltration

2010 ◽  
Vol 43 (3) ◽  
pp. 788-796 ◽  
Author(s):  
Laura T. Rodríguez Furlán ◽  
Antonio Pérez Padilla ◽  
Mercedes E. Campderrós
Keyword(s):  
Plasma Proteins ◽  
Bovine Plasma

scholarly journals Antioxidant Effect of Bovine Plasma Proteins Modified via Maillard Reaction on n3 Fortified Beef Patties

2016 ◽  
Vol 07 (08) ◽  
pp. 671-681 ◽  
Author(s):  
Carina Lorena Fernández ◽  
Ricardo Alejandro Fogar ◽  
Mirtha Marina Doval ◽  
Ana María Romero ◽  
María Alicia Judis
Keyword(s):  
Maillard Reaction ◽  
Plasma Proteins ◽  
Antioxidant Effect ◽  
Beef Patties ◽  
Bovine Plasma

Binding Affinity of Purified Plasma Proteins for Phenethylbiguanide, an Oral Hypoglycemic Compound

1958 ◽  
Vol 4 (6) ◽  
pp. 496-509 ◽  
Author(s):  
Herndon G Shepherd ◽  
Hugh J McDonald
Keyword(s):  
Binding Affinity ◽  
Plasma Proteins ◽  
Equilibrium Dialysis ◽  
Colorimetric Method ◽  
Thermodynamic Activity ◽  
Plasma Albumin ◽  
Hypoglycemic Agent ◽  
Native Proteins ◽  
Bovine Plasma

Abstract A colorimetric method has been adapted to the quantitative determination of the oral hypoglycemic compound phenethylbiguanide. This method was useful in studying the binding affinity of purified bovine plasma albumin and gamma globulin for the hypoglycemic agent. Equilibrium dialysis studies, which measure the decrease in thermodynamic activity of the bound cation, reveal that there is no significant interaction between phenethylbiguanide and the two native proteins. Consequently, the two plasma proteins are assumed to exert no buffering action in controlling the plasma concentration of the drug. The adherence of phenethylbiguanide to Beer's Law indicates that the compound exists in the monomeric state in aqueous solution below 10-4 molar.

Surimi Gel Enhancement by Bovine Plasma Proteins

1997 ◽  
Vol 45 (8) ◽  
pp. 2919-2923 ◽  
Author(s):  
Thomas A. Seymour ◽  
Margo Y. Peters ◽  
Michael T. Morrissey ◽  
Haejung An
Keyword(s):  
Plasma Proteins ◽  
Surimi Gel ◽  
Bovine Plasma

scholarly journals MODELAMIENTO DE LA CINÉTICA DE HIDRÓLISIS ENZIMÁTICA DE PROTEÍNAS DEL PLASMA BOVINO (MODELING OF THE KINETICS OF ENZYMATIC HYDROLYSIS OF BOVINE PLASMA PROTEINS)

Revista EIA ◽  
2013 ◽  
Vol 9 (17) ◽  
pp. 71
Author(s):  
Omar Alfredo Figueroa ◽  
José Édgar Zapata ◽  
Gail Albeiro Gutiérrez
Keyword(s):  
Kinetic Model ◽  
Plasma Proteins ◽  
Batch Reactor ◽  
Degree Of Hydrolysis ◽  
Order Kinetic ◽  
Enzyme Substrate ◽  
Bovine Plasma ◽  
Order Kinetic Model ◽  
Rate Of Hydrolysis ◽  
Hydrolysis Of

Se utilizó un modelo cinético para estudiar la velocidad de reacción en la hidrólisis de proteínas de plasma de bovino con alcalasa 2,4 L en un reactor batch. Se estudió la influencia de variables como la concentración inicial de sustrato y enzima sobre el grado de hidrólisis y se determinaron los parámetros cinéticos de la ecuación de velocidad, analizando su relación con las variables de trabajo. Se ajustó un modelo cinético de orden cero y desactivación enzimática por sustrato, de segundo orden, así como la relación directa entre la fracción enzima-sustrato y la tasa de formación de productos de hidrólisis.Abstract: A kinetic model was used to study the reaction rate of hydrolysis of bovine plasma proteins and alcalase 2.4 L, in a batch reactor. The influence of variables, such as the concentration of initial enzyme substrate and the degree of hydrolysis was studied, and kinetic parameters of the rate equation were determined by analyzing its relationship with the work variables. A zero-order kinetic model and enzyme deactivation by substrate was found, as well as the direct relationship between the fraction of enzyme-substrate and the rate of formation of hydrolysis products.

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