scholarly journals Milk and Meat Allergens from Bos taurus β-Lactoglobulin, α-Casein, and Bovine Serum Albumin: An In-Vivo Study of the Immune Response in Mice

Nutrients ◽  
2019 ◽  
Vol 11 (9) ◽  
pp. 2095 ◽  
Author(s):  
Ewa Fuc ◽  
Dagmara Złotkowska ◽  
Barbara Wróblewska
Keyword(s):  
Immune Response ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cellular Response ◽  
Cow Milk ◽  
Mice Model ◽  
Beef Meat ◽  
Β Lactoglobulin

The mechanism of food allergy may vary. This study aimed to compare the effects of milk, yogurt, or beef meat supplementation on humoral and cellular immune responses in a mice model. Mice were divided into four groups: The “Milk group” was sensitized with a β-lactoglobulin (β-lg)/α-casein (α-CN) mixture and supplemented cow milk; the “Yogurt group” was sensitized with β-lg/α-CN and supplemented yogurt; the “Beef group” was immunized with bovine serum albumin (BSA) and supplemented beef meat; and the “PBS group” received PBS in all procedures. ELISA was used to measure humoral response, including: Total IgE, specific IgG, and IgA. Cellular response was determined by phenotyping lymphocyte from lymphoid tissue and measuring the Th1/Th2 cytokine concentration with flow cytometry. The qPCR method was used for quantification of the fecal microbiota. The results obtained revealed a lower IgE level for the Yogurt group than for the Milk one. In the Yogurt group, the contribution of regulatory T cells to MLN and PP was higher compared to the other groups. We confirmed that diet supplementation with yogurt modulates the immune response to the prime allergen, and changes the activity of serum antibodies to milk proteins and BSA. Based on a specific antibodies level, we cannot exclude the possibility of CMA mice reaction against BSA.

Correlations between the content of selected whey proteins in cow milk

2017 ◽  
Vol 13 (1) ◽  
pp. 33-45
Author(s):  
Aneta Brodziak ◽  
Jolanta Król ◽  
Anna Litwińczuk ◽  
Anna Wolanciuk
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Whey Proteins ◽  
Correlation Coefficients ◽  
Hplc Method ◽  
Cow Milk ◽  
Black And White ◽  
Scatter Plots ◽  
Β Lactoglobulin

The aim of the study was to determine the correlations between the concentrations of major whey proteins in cow milk. A total of 2,278 milk samples from Polish Holstein-Friesian (Black-and-White and Red-and-White varieties), Simmental and Jersey cows were analysed. In each sample the content of major whey proteins, i.e. α-lactalbumin, β-lactoglobulin, bovine serum albumin, lactoferrin and lysozyme were determined by the RP-HPLC method. Matrix scatter plots were prepared to determine the correlations between the concentrations of individual whey proteins. In the vast majority of cases a significant relationship was found between the content of individual whey proteins. Taking into account the production season and breed of cow, highly significant (p=0.001) negative correlation coefficients were obtained for the content of α-lactalbumin and bovine serum albumin, for α-lactalbumin and lysozyme, for β-lactoglobulin and bovine serum albumin, and for β-lactoglobulin and lysozyme. Positive correlations were observed for the concentrations of α-lactalbumin with β-lactoglobulin, lactoferrin and lysozyme, as well as for bovine serum albumin with lysozyme.

UCNP@BSA@Ru nanoparticles with tumor-specific and NIR-triggered efficient PACT activity in vivo

2021 ◽  
Author(s):  
Chao Zhang ◽  
Xusheng Guo ◽  
Xuwen Da ◽  
Yishan Yao ◽  
Haihua Xiao ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Short Wavelength ◽  
Ru Nanoparticles ◽  
Wavelength Absorption ◽  
Tumor Accumulation ◽  
Accumulation Ability

Ru(II)-based photoactivated chemotherapy (PACT) agents are promising, however, the short wavelength absorption (generally < 550 nm) and poor tumor accumulation ability limit their in vivo applications. Herein bovine serum albumin...

BSA directed-synthesis of biocompatible Fe3O4 nanoparticles for dual-modal T1 and T2 MR imaging in vivo

2017 ◽  
Vol 9 (21) ◽  
pp. 3099-3104 ◽  
Author(s):  
Dong Li ◽  
Minghui Hua ◽  
Kun Fang ◽  
Rong Liang
Keyword(s):  
Bovine Serum Albumin ◽  
Mr Imaging ◽  
Serum Albumin ◽  
Fe3o4 Nanoparticles ◽  
Bovine Serum ◽  
Mild Conditions ◽  
Directed Synthesis ◽  
T1 And T2

Bovine serum albumin-Fe3O4 nanoparticles with undoubted biosafety and robust dual-modal T1 and T2 MR imaging ability were fabricated using a biomineralization approach in a facile way under mild conditions for in vivo MR imaging.

scholarly journals Clearance and binding of native and defucosylated lactoferrin

1983 ◽  
Vol 212 (2) ◽  
pp. 249-257 ◽  
Author(s):  
M J Imber ◽  
S V Pizzo
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Binding ◽  
Gel Filtration ◽  
Peritoneal Macrophages ◽  
Mononuclear Phagocyte ◽  
Stable Complex

These studies explore the role of carbohydrate recognition systems and the direct involvement of terminal alpha 1-3-linked fucose in the clearance of lactoferrin from the murine circulation and in the specific binding of lactoferrin to receptors on murine peritoneal macrophages. As previously reported, radiolabelled lactoferrin cleared very rapidly (t1/2 less than 1 min) after intravenous injection into mice. However, competing levels of ligands specific for the hepatic galactose receptor (asialo-orosomucoid), the hepatic fucose receptor (fucosyl-bovine serum albumin), and the mononuclear-phagocyte system pathway recognizing mannose, N-acetylglucosamine and fucose (mannosyl-, N-acetylglucosaminyl- and fucosyl-bovine serum albumin) did not block radiolabelled lactoferrin clearance in vivo or binding to mouse peritoneal macrophage monolayers in vitro. Almond emulsin alpha 1-3-fucosidase was used to prepare defucosylated lactoferrin in which 88% of the alpha 1-3-linked fucose was hydrolysed. No difference in clearance or receptor binding was observed between radiolabelled native and defucosylated lactoferrin. Fucoidin, a fucose-rich algal polysaccharide, completely inhibits the clearance in vivo and macrophage binding in vitro of lactoferrin. This effect, however, is probably not the result of competition for binding to the fucose receptor, since gel-filtration studies demonstrated formation of a stable complex between lactoferrin and fucoidin. The present results indicate that the lactoferrin-clearance pathway is distinct from several pathways mediating glycoprotein clearance through recognition of terminal galactose, fucose, N-acetylglucosamine or mannose. Furthermore, alpha 1-3-linked fucose on lactoferrin is not essential for lactoferrin clearance in vivo or specific binding to macrophage receptors in vitro.

Corona protein impacts on alternating current biosusceptometry signal and circulation times of differently coated MnFe2O4 nanoparticles

Nanomedicine ◽  
2021 ◽  
Author(s):  
Andre Gonçalves Prospero ◽  
Lais Pereira Buranello ◽  
Carlos AH Fernandes ◽  
Lucilene Delazari dos Santos ◽  
Guilherme Soares ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Signal Intensity ◽  
Alternating Current ◽  
Circulation Time ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

Background: We evaluated the impacts of corona protein (CP) formation on the alternating current biosusceptometry (ACB) signal intensity and in vivo circulation times of three differently coated magnetic nanoparticles (MNP): bare, citrate-coated and bovine serum albumin-coated MNPs. Methods: We employed the ACB system, gel electrophoresis and mass spectrometry analysis. Results: Higher CP formation led to a greater reduction in the in vitro ACB signal intensity and circulation time. We found fewer proteins forming the CP for the bovine serum albumin-coated MNPs, which presented the highest circulation time in vivo among the MNPs studied. Conclusion: These data showed better biocompatibility, stability and magnetic signal uniformity in biological media for bovine serum albumin-coated MNPs than for citrate-coated MNPs and bare MNPs.

Chemotactic properties, cellular binding and uptake of peptides and peptide derivatives: studies with Tetrahymena thermophila

1992 ◽  
Vol 103 (2) ◽  
pp. 565-570
Author(s):  
V. Leick
Keyword(s):  
Bovine Serum Albumin ◽  
Cell Surface ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Tetrahymena Thermophila ◽  
Chemotactic Peptide ◽  
Dansyl Group ◽  
Peptide Derivatives

Receptor-mediated binding of leukocyte chemotactic peptide, N-formylMet-Leu-Phe (fMLP), occurs in the ciliated protozoon Tetrahymena thermophila. In vivo labelling of the cells with N-formylMet-Leu-[3H]Phe ([3H]fMLP) shows that the cells bind the ligand with high affinity (KD = 4 × 10(−9) M to 1 × 10(−8) M). Moreover, Scatchard transformations of the binding data show that there are about 5 × 10(5) binding sites per cell on the cell surface. Two fluorescent derivatives of leukocyte chemotactic peptide, N-dansylMet-Leu-Phe (dansMLP) and N-formylMet-Leu-Phe-(N-dansyl-)Lys (fMLPdanLys) compete for the N-formylMet-Leu-Phe (fMLP) binding sites on the cell surface. Moreover, both derivatives have retained significant chemoattracting potentials. Fluorescence from dansMLP, but not from fMLPdansLys and dansyl-beta-endorphin, is internalized preferentially into small vesicles. The differences may, however, reflect that the fluorescence from the dansyl group is strongly quenched by a hydrophilic microenvironment when using the two latter peptide derivatives. In contrast, the dansyl group from dansMLP must be assumed to be embedded in a hydrophobic microenvironment in the vesicular membrane or membrane protein. Rhodamine-labelled bovine serum albumin, egg albumin and cytochrome c as well as dansylated bovine serum albumin, which are poor chemoattractants, are preferentially seen to be internalized into large vesicles (food vacuoles).

Rhamnose modified bovine serum albumin as a carrier protein promotes the immune response against sTn antigen

2020 ◽  
Vol 56 (90) ◽  
pp. 13959-13962
Author(s):  
Han Lin ◽  
Haofei Hong ◽  
Jinfeng Wang ◽  
Chen Li ◽  
Zhifang Zhou ◽  
...  
Keyword(s):  
Immune Response ◽  
Bovine Serum Albumin ◽  
Immune Responses ◽  
Serum Albumin ◽  
Cancer Vaccine ◽  
Bovine Serum ◽  
Vaccine Development ◽  
Carrier Protein ◽  
Antigen Uptake ◽  
Specific Antibodies

Rhamnose and sTn antigen were co-conjugated to bovine serum albumin (BSA) for cancer vaccine development. The immune responses against sTn have been significantly augmented with the involvement of Rha-specific antibodies to enhance antigen uptake.

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