scholarly journals STUDIES ON ANTIBODY PRODUCTION

1963 ◽  
Vol 117 (6) ◽  
pp. 1053-1062 ◽  
Author(s):  
Thomas F. O'Brien ◽  
Maria C. Michaelides ◽  
Albert H. Coons
Keyword(s):  
Lymph Node ◽  
Bovine Serum Albumin ◽  
Antibody Response ◽  
Antibody Production ◽  
Bovine Serum ◽  
Time Course ◽  
Antibody Synthesis ◽  
Anamnestic Response

The in vitro anamnestic antibody response of popliteal lymph node fragments to additions of antigen closely resembles the in vivo anamnestic antibody response in its sensitivity to antigen, in the time course of antibody production, and in the sequence of appearance and the morphology of the antibody containing cells. Most of the cells responsible for antibody synthesis remain in the explant and do not migrate, although a few can be found in the outgrowing sheet of cells. The smallest concentration of bovine serum albumin which stimulates an anamnestic response in vitro is about 1 x 10–9 gm/ml.

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.

scholarly journals THE X-Y-Z SCHEME OF IMMUNOCYTE MATURATION

1968 ◽  
Vol 127 (2) ◽  
pp. 307-325 ◽  
Author(s):  
Vera S. Byers ◽  
Eli E. Sercarz
Keyword(s):  
Lymph Node ◽  
Antibody Response ◽  
Lymph Nodes ◽  
Large Dose ◽  
Primary Response ◽  
Memory Cells ◽  
Secondary Antibody ◽  
Booster Injection

A set of conditions has been described under which primed rabbit lymph nodes produce a secondary antibody response upon in vivo stimulation with a large dose of antigen, but are subsequently "exhausted;" that is, lymph node cultures prepared at intervals following the booster injection cannot be re-stimulated to display tertiary responses. Rabbits given 100-fold less antigen in the booster inoculum were able to give a tertiary response upon in vitro challenge. The system used permits neither induction nor continuation of a primary response to BSA in vitro. Since it could be demonstrated that no memory cells were generated by the booster injection within the intervals between in vivo injection and culture, the tertiary response in nonexhausted nodes must have been due to residual memory cells which remained untriggered by the in vivo booster injection. The unresponsive state was not caused by antibody feedback. These results are interpreted to mean that a population of memory cells can be exhausted by a supraoptimal dose of antigen, rendering the node temporarily incapable of further response. This implies that long-lived memory is not due to asymmetric division of memory cells. The source and fate of memory cells is discussed with regard to this evidence.

scholarly journals REGULATION OF THE IMMUNE SYSTEM BY SYNTHETIC POLYNUCLEOTIDES

1972 ◽  
Vol 135 (1) ◽  
pp. 45-67 ◽  
Author(s):  
Robert D. Stout ◽  
Arthur G. Johnson
Keyword(s):  
Immune System ◽  
Bovine Serum Albumin ◽  
Antibody Production ◽  
Bovine Serum ◽  
Culture Medium ◽  
Complex Form ◽  
Spleen Cells ◽  
Fourfold Increase ◽  
Polyuridylic Acid

Addition of polyadenylic-polyuridylic acid in complex form (poly A:U) without antigen to a suspension of spleen cells obtained from BALB/Aj mice primed 6 wk previously with human γ-globulin (HGG) resulted in an immediate fourfold increase over background number of anti-HGG rosette-forming cells (RFC). Culture of similar cells in the presence of puromycin for 1–6 hr before poly A:U did not significantly reduce the response. Continued culture of primed spleen cells in the presence of poly A:U, resulted in a decrease of RFC to background levels within an hour followed by an increase again 6 hr later. This later increase in RFC was inhibited by addition of puromycin to the culture medium. The nonspecific stimulation by poly A:U of antibody production by primed spleen cells also was induced in vivo. Increases in splenic RFC were detectable 6 hr after intravenous injection of poly A:U alone, without antigen, into primed mice. The response peaked at 18 hr and had dissipated completely within 3 days. A second injection of poly A:U 24 hr or later after the first injection resulted in a second response, similar to the first with respect to kinetics and intensity. Rosette formation by poly A:U-stimulated cells could not be inhibited by mitotic poisons, but was inhibited by treatment of the cells with goat anti-mouse γ-globulin serum, suggesting that the antibody involved was a 7S γ-globulin. The decrease in RFC induced by culture of primed cells for 1 hr in poly A:U paralleled a decrease in secondary responsiveness of the cells to antigen. This poly A:U-induced inhibition of secondary responsiveness could be reversed by suspending the treated cells in supernatant fluids derived from poly A:U-stimulated cultures. The reversal was specific in that supernatant fluids removed from bovine serum albumin (BSA)-primed cells by poly A:U did not stimulate the response of HGG-primed cells to HGG. However supernatant fluids from BSA-primed cells caused the production of anti-HGG RFC if BSA rather than HGG was used as triggering antigen. The active factor in the supernatant fluids appeared to be a 7S γ-globulin since activity was lost after 45 min incubation of the supernatant fluids in the presence of goat anti-mouse 7S γ-globulin serum.

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 THE X-Y-Z SCHEME OF IMMUNOCYTE MATURATION

1968 ◽  
Vol 128 (4) ◽  
pp. 715-728 ◽  
Author(s):  
Vera S. Byers ◽  
Eli E. Sercarz
Keyword(s):  
Bovine Serum Albumin ◽  
Antibody Response ◽  
Serum Albumin ◽  
Lymph Nodes ◽  
Bovine Serum ◽  
Antibody Formation ◽  
Memory Cell ◽  
Secondary Response ◽  
Antigen Concentration

A concentration of 5 mg/ml bovine serum albumin (BSA) prevents the in vitro elicitation of a secondary response in primed rabbit popliteal lymph nodes, if it is left in contact with the node fragments for the first 6 days of culture. No antibody formation can be detected at any time during the culture period in most cases, although occasional fragments are resistant to inhibition. Reducing the exposure time to the first 3 days of culture delays the peak of the antibody response. The inhibition is antigen specific. Reconstruction experiments demonstrate that the inhibition is not due to antigen masking of the antibody. Even shortly after optimal stimulation, the addition of 5 mg/ml BSA to the fragments was not able to prevent a normal antibody response. The implications of these findings are that (a) a high antigen concentration suspends the memory cell in a reversibly paralyzed state, (b) memory cells have a heterogeneous susceptibility to inhibition, (c) once induced, the antibody response cannot be inhibited by antigen overloading, (d) unresponsiveness in a primed animal can be due to either exhaustion of the memory cell population or paralysis of the memory cell.

scholarly journals The biosynthesis of phosphatidic acid and phosphatidylinositol in mammalian pancreas

1967 ◽  
Vol 105 (1) ◽  
pp. 379-392 ◽  
Author(s):  
C. Prottey ◽  
J. N. Hawthorne
Keyword(s):  
Fatty Acids ◽  
Bovine Serum Albumin ◽  
Guinea Pig ◽  
Phosphatidic Acid ◽  
Bovine Serum ◽  
Intraperitoneal Injection ◽  
Synthetase Activity ◽  
Absolute Requirement

1. The labelling of guinea-pig pancreas phospholipids in vivo after intraperitoneal injection of [32P]orthophosphate is described. 2. Acyl-CoA synthetase activity in pancreas homogenates has been studied. There is no absolute requirement for added fatty acids, indicating an adequate supply of endogenous fatty acids in these preparations. 3. Phosphatidic acid is formed in guinea-pig pancreas preparations by two distinct routes, namely the acylation of l-3-glycerophosphate and the phosphorylation of 1,2-diglyceride. Phosphatidic acid formed by either mechanism is converted into phosphatidylinositol by guinea-pig pancreas in vitro. 4. The enzymes of pancreas that convert phosphatidic acid into phosphatidylinositol via CDP-diglyceride have been characterized. 5. Addition of bovine serum albumin is necessary in assaying certain of these enzymes.

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.

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