Photochemical immobilization of bovine serum albumin on Ti–O and evaluations in vitro and in vivo

2008 ◽  
Vol 255 (2) ◽  
pp. 489-493 ◽  
Author(s):  
Y.J. Weng ◽  
F. Qi ◽  
N. Huang ◽  
J. Wang ◽  
J.Y. Cheng ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

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.

Oxygen concentration and protein source affect the development of preimplantation goat embryos in vitro

1991 ◽  
Vol 3 (5) ◽  
pp. 601 ◽  
Author(s):  
PA Batt ◽  
DK Gardner ◽  
AW Cameron
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Oxygen Concentration ◽  
Bovine Serum ◽  
Calf Serum ◽  
Cell Number ◽  
The Mean ◽  
Number Of Cells

The effect of oxygen concentration and the source of protein in culture medium on the development of 2- to 4-cell goat embryos in vitro was investigated. Embryos were collected from superovulated Angora-Cashmere-cross goats 48 h after ovulation and cultured for 6 days in synthetic oviduct fluid (SOF) medium under one of two oxygen concentrations (20% or 7%) and in the presence of one of five protein sources; Miles bovine serum albumin (Miles BSA), Commonwealth Serum Laboratory bovine serum albumin (CSL BSA), goat serum (GS), fetal calf serum (FCS) and human serum (HS). In the presence of 20% oxygen the percentage of embryos reaching the expanded and/or hatched blastocyst stage in SOF medium containing Miles BSA was 29%, with a mean cell number per embryo of 28.1 +/- 6.0 (+/- s.e.m.). Use of an oxygen concentration of 7% significantly increased the percentage of embryos reaching this stage (80%, P less than 0.01) and the mean number of cells per embryo (65.3 +/- 8.2, P less than 0.01). The mean number of cells of the early-cleavage-stage embryos was significantly lower when the medium contained CSL BSA, GS or FCS (42.7 +/- 5.6, 29.0 +/- 6.1 and 21.3 +/- 3.2, respectively) than with Miles BSA (92.8 +/- 6.4) or HS (104.8 +/- 17.2) (P less than 0.01). Under 7% oxygen and with Miles BSA or HS, embryos were morphologically comparable to those developed in vivo, but the mean cell numbers in vitro were only approximately half those obtained in vivo.

scholarly journals Effect of soya-bean protein on meat iron solubility and absorption in rats

1986 ◽  
Vol 55 (2) ◽  
pp. 419-426 ◽  
Author(s):  
G. O. Latunde-Dada ◽  
R. J. Neale
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
In Vitro Digestion ◽  
Soya Bean ◽  
Chicken Meat ◽  
Iron Solubility ◽  
Bean Protein

1. Soya-bean proteins were used to replace 30 and 50% of the protein from 59Fe-labelled pigeon (Columbn L.) and chicken meat, and the solubility of the meat 59Fe in vitro and its absorption in vivo in rats in the presence and absence of soya-bean proteins were measured.2. Replacement of part of the chicken meat by soya-bean proteins reduced 59Fe solubility from chicken meat at all stages during simulated in vitro digestion.3. 59Fe absorption from 59Fe-labelled chicken meat when given to both Fe-replete and Fe-deficient rats was reduced in the presence of soya-bean proteins but was unaffected by the presence of casein or bovine serum albumin. 59Fe-absorption from pigeon meat in the presence of soya-bean proteins was not reduced to the same extent as that from chicken meat.4. There was no significant effect of soya-bean proteins on 59Fe-labelled haemoglobin Fe absorption in vivo in Fe-replete rats.5. Absorption of 59Fe from the isolated haemoproteins from chicken meat was unaffected by soya-bean proteins but 59Fe absorption from the main non-haem-Fe fractions was strongly inhibited, particularly from haemosiderin.

scholarly journals Implication of the deacetylase sirtuin-1 on synovial angiogenesis and persistence of experimental arthritis

2020 ◽  
Vol 79 (7) ◽  
pp. 891-900 ◽  
Author(s):  
Agathe Leblond ◽  
Sonia Pezet ◽  
Anne Cauvet ◽  
Claudine Casas ◽  
Julie Pires Da Silva ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Sirtuin 1 ◽  
Matricellular Protein ◽  
Sirt1 Expression ◽  
Tnf Α ◽  
Activated State

ObjectivesTo decipher the phenotype of endothelial cells (ECs) derived from circulating progenitors issued from patients with rheumatoid arthritis (RA).MethodsRA and control ECs were compared according to their proliferative capacities, apoptotic profile, response to tumour necrosis factor (TNF)-α stimulation and angiogenic properties. Microarray experiments were performed to identify gene candidates relevant to pathological angiogenesis. Identified candidates were detected by RT-PCR and western blot analysis in ECs and by immunohistochemistry in the synovium. Their functional relevance was then evaluated in vitro after gene invalidation by small interfering RNA and adenoviral gene overexpression, and in vivo in the mouse model of methyl-bovine serum albumin-(mBSA)-induced arthritis.ResultsRA ECs displayed higher proliferation rate, greater sensitisation to TNF-α and enhanced in vitro and in vivo angiogenic capacities. Microarray analyses identified the NAD-dependent protein deacetylase sirtuin-1 (SIRT1) as a relevant gene candidate. Decreased SIRT1 expression was detected in RA ECs and synovial vessels. Deficient endothelial SIRT1 expression promoted a proliferative, proapoptotic and activated state of ECs through the acetylation of p53 and p65, and lead the development of proangiogenic capacities through the upregulation of the matricellular protein cysteine-rich angiogenic protein-61. Conditional deletion of SIRT1 in ECs delayed the resolution of experimental methyl-bovine serum albumin-(mBSA)-induced arthritis. Conversely, SIRT1 activation reversed the pathological phenotype of RA ECs and alleviates signs of experimental mBSA-induced arthritis.ConclusionsThese results support a role of SIRT1 in RA and may have therapeutic implications, since targeting angiogenesis, and especially SIRT1, might be used as a complementary therapeutic approach in RA.

scholarly journals In vivo and in vitro biocompatibility study of novel microemulsion hybridized with bovine serum albumin as nanocarrier for drug delivery

Heliyon ◽  
2019 ◽  
Vol 5 (6) ◽  
pp. e01858 ◽  
Author(s):  
Mahmoud Gharbavi ◽  
Hamidreza Kheiri Manjili ◽  
Jafar Amani ◽  
Ali Sharafi ◽  
Hossein Danafar
Keyword(s):  
Drug Delivery ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
In Vitro Biocompatibility ◽  
Biocompatibility Study
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