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Bovine serum albumin

About: Bovine serum albumin is a research topic. Over the lifetime, 19981 publications have been published within this topic receiving 571291 citations. The topic is also known as: BSA.


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Journal ArticleDOI
TL;DR: It is recommended that all mouse monoclonal two-site assays should contain non-immune mouse serum (or a suitable "irrelevant" mouse monOClonal antibody) to prevent false-positive results.
Abstract: With a two-site CK-MB assay, we screened serum samples from 1008 blood donors for the presence of antibodies to mouse monoclonal immunoglobulin. These antibodies were capable of cross-linking the labeled antibody with the solid-phase antibody in the two-site assay, thus generating a falsely high apparent CK-MB concentration. In 92 (9.12%) of the blood donors tested, apparent CK-MB concentrations of 10-1000 micrograms/L decreased to less than 3 micrograms/L when re-assayed with non-immune mouse serum (10 mL/L) included in the assay reagent. We tested the ability of non-immune sera from other animal species to lower the concentration of apparent CK-MB in 58 of the 92 samples. Bovine and ovine serum were almost as effective as mouse serum; feline, canine, and rabbit serum were less effective. Of the samples tested, 12% (1.1% of the original population screened) showed apparent CK-MB values that either were not depressed by bovine serum or were only partly depressed. We discuss the possible etiology of these antibodies in normal subjects and recommend that all mouse monoclonal two-site assays should contain non-immune mouse serum (or a suitable "irrelevant" mouse monoclonal antibody) to prevent false-positive results.

131 citations

Journal ArticleDOI
TL;DR: A novel blend of polycaprolactone and bovine serum albumin (BSA) to form nanofibers containing nerve growth factors is shown, demonstrating the successful incorporation and controlled release potential of PCL BSA scaffolds.

131 citations

Journal Article
TL;DR: A mechanism by which to explain the metabolic fate and distribution of NO among thiol pools in the vasculature is suggested, and S-transnitrosation at the cell surface in NO signal transduction is implicate.
Abstract: S-Nitrosothiols are a group of potent, bioactive compounds that form through the reaction of nitric oxide (NO) with thiols in the presence of oxygen. These compounds are naturally occurring in vivo, stabilize NO and potentiate its biological effects. S-Nitrosoglutathione is the most abundant intracellular S-nitrosothiol, and the kinetics for its formation favors de novo synthesis. In this analysis, we studied the formation of S-nitrosothiols by S-transnitrosation, or exchange of -NO for -H between sulfur atoms; we synthesized S-nitroso-glutathionyl-Sepharose 4B beads (SNO-4B) as a reagent with which to measure S-transnitrosation reactions. We detected a maximum of 1.57 +/- 0.24 pmol NO/bead (n = 5) after S-nitrosation of the beads with acidified nitrite. The stability of the S-NO bond was dependent on temperature, but not pH over the 5 to 9 range (except at pH 9 at 37 degrees ), with an estimated t1/2 of 30 hr at 22 degrees C and of approximately 2 wk at 4 degrees C. We demonstrated that SNO-4B transfers -NO to glutathione and to cysteine rapidly and in a pH-dependent manner. The initial rate of transfer of -NO from SNO-4B to glutathione at room temperature was 0.53, 3.03 and 5.14 microM/min at pH 5.0, 7.4 and 9.0, respectively (P < .05). Under the same conditions, the initial rate of -NO transfer to cysteine was 0. 72, 3.71 and 4.69 microM/min at pH 5.0, 7.4 and 9.0, respectively (P < .05). There was no appreciable S-transnitrosation between SNO-4B and bovine serum albumin. We further demonstrated that SNO-4B evokes significant vasodilator and platelet inhibitory responses in plasma-free systems and activates platelet soluble guanylyl cyclase. These data suggest a mechanism by which to explain the metabolic fate and distribution of NO among thiol pools in the vasculature, and implicate S-transnitrosation at the cell surface in NO signal transduction.

131 citations

Journal ArticleDOI
TL;DR: In this article, the concentration dependence of surface tension was evaluated with DuNouy ring tensiometry for solutions of α-lactalbumin (α-Lac), β-Lactoglobulin (β-Lg), and bovine serum albumin (BSA).

130 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023475
2022983
2021423
2020460
2019468
2018489