scholarly journals pH-dependent binding of immunoglobulins to intestinal cells of the neonatal rat.

1976 ◽  
Vol 71 (2) ◽  
pp. 666-669 ◽  
Author(s):  
R Rodewald
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Neonatal Rat ◽  
Intestinal Cells ◽  
Luminal Surface ◽  
Rabbit Igg ◽  
Old Rats ◽  
Histochemical Marker ◽  
Ph Dependent

Rat and rabbit IgG immunoglobulins conjugated to horseradiah peroxidase as a histochemical marker bind at 0 degrees C to the luminal surface of absorptive cells in isolated segments of jejunum from 10-12-day old rats. Binding is observed at pH 6.0, near the normal luminal pH of the duodenum and jejunum at this age, but not at pH 7.4. Furthermore, no binding occurs when cells are exposed at pH 6.0 to either free peroxidase or peroxidase conjugated to chicken or sheep IgG immunoglobulins or bovine serum albumin. The sensitivity of binding to pH suggests a means whereby immunoglobulins which are selectively absorbed by the cells can be released efficiently at the abluminal surface.

A solid-phase enzymeimmunoassay for the determination of progesterone in bovine, porcine and ovine plasma

1995 ◽  
Vol 75 (4) ◽  
pp. 525-529 ◽  
Author(s):  
R. P. Del Vecchio ◽  
W. D. Sutherland ◽  
M. L. Connor
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Petroleum Ether ◽  
Bovine Serum ◽  
Solid Phase ◽  
Plasma Samples ◽  
Assay Sensitivity ◽  
Coefficients Of Variation ◽  
Rabbit Igg

The purpose of this project was to develop a valid quantitative enzymeimmunoassay (EIA) for progesterone in blood plasma of cattle, pigs and sheep. Rabbit anti-progesterone, mouse monoclonal anti-rabbit IgG, authentic progesterone, and acetylcholine esterase bound covalently to progesterone were the principal reagents used to develop the EIA. Ninety-six well microliter plates were coated with mouse monoclonal anti-rabbit IgG and saturated with bovine serum albumin before use. Rabbit anti-progesterone was diluted to a working dilution of 1:2.0 × 106. Standard curves were linear and ranged from 1.56 to 400 pg of progesterone per well which allowed for the measurement of 0.03125 to 8.0 ng mL−1. Assay sensitivity averaged 1.56 pg well−1. Progesterone was extracted from plasma samples with petroleum ether. Plasma samples (n = 3 or 4 from each species) with unknown amounts of progesterone that were extracted and serially diluted with EIA buffer did not deviate from parallelism with progesterone standard curves in buffer. The correlation between EIA and radioimmunoassay (RIA) measurements of progesterone in the same plasma samples was high (P < 0.0001) for all three species (r = 0.96 for bovine; r = 0.96 for porcine; r = 0.94 for ovine). The regression of EIA data on RIA data produced the following equations:[Formula: see text]The intra- and inter-assay coefficients of variation were 5.4 and 10.6% for bovine, 5.8 and 11.0% for porcine and, 6.1 and 12.3% for ovine, respectively. These data show that this EIA is a valid and reliable memod for quantitating progesterone in extracts of bovine, porcine and ovine plasma. Key words: Enzymeimmunoassay, progesterone, plasma, bovine, porcine, ovine

Isotachophoretic analysis of the pH dependent carrier properties of bovine serum albumin for rifamycin AF/013

1986 ◽  
Vol 7 (10) ◽  
pp. 447-453
Author(s):  
Adam Csordas ◽  
Peter Josef Oefner ◽  
Georg Bartsch ◽  
Hans Grunicke ◽  
Giancarlo Lancini
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ph Dependent

Investigation on the pH-dependent binding of Eosin Y and bovine serum albumin by spectral methods

2007 ◽  
Vol 127 (2) ◽  
pp. 515-522 ◽  
Author(s):  
Dejiang Gao ◽  
Yuan Tian ◽  
Fanghui Liang ◽  
Danhong Jin ◽  
Yanhua Chen ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Spectral Methods ◽  
Bovine Serum ◽  
Eosin Y ◽  
Ph Dependent

scholarly journals pH DEPENDENT STRUCTURES OF BOVINE SERUM IN SOLUTION BY SMALL ANGLE NEUTRON SCATTERING

2021 ◽  
Vol 83 (2) ◽  
pp. 117-123
Author(s):  
Arum Patriati ◽  
Edy Giri Rachman Putra
Keyword(s):  
Crystal Structure ◽  
Protein Structure ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Neutron Scattering ◽  
Small Angle ◽  
Bovine Serum ◽  
Small Angle Neutron Scattering ◽  
Static State ◽  
Ph Dependent

The pH-dependent structures of the bovine serum albumin (BSA), under physiological conditions that permit enzymatic activity, were investigated by small-angle neutron scattering (SANS). The unfolding behavior of BSA in solution is important to understand the mechanism of protein aggregation due to protein conformational change. The information of protein structure is crucial to design the perfect protein-based drug delivery device. This information will be useful as a complementary data of BSA crystal structure in static state. The structure of BSA in solution was found to be heart shaped, nearly identical to bovine serum albumin crystal structure. The globular heart shaped structure of BSA was still maintained at alkaline pH range of 7 to 11. It underwent partial unfolding at pH 5 and continued to unfold at pH 3. The unfolded-structure of BSA shows that the globular structure started to change into a cylinder-like structure at pH 3 which was clearly shown in Kratky plot. These results were confirmed with ab initio low-resolution shape calculation model analysis using GNOM and DAMMIF in obtaining the three-dimensional protein structure model.

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