Topic
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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TL;DR: A quantitatively similar degree of protein yields was obtained for the beta-galactoside-binding protein of bovine heart, although different proteins were obtained when neoglycoproteins were used as ligand.
166 citations
TL;DR: It is proposed that IGFBP-3 serves a dual function in modulating IGF action in vivo by sequestering and preventing IGF-I receptor binding, whereas surface-associated bIGF BP-3 enhances the growth-promoting effects of IGF-i in bovine fibroblasts.
Abstract: Insulin-like growth factor binding protein-3 (IGFBP-3) purified from bovine serum shares 19 of 25 amino-terminal amino acid residues with IGFBP-3 purified from human, rat, and porcine sources. A newly characterized bovine fibroblast model was used to investigate the biological effects of purified bovine IGFBP-3 (bIGFBP-3). Coincubation of insulin-like growth factor I (IGF-I) with increasing concentrations of bIGFBP-3 produced a dose-dependent inhibition of IGF-I-stimulated [3H]aminoisobutyric acid (AIB) uptake in cultured bovine fibroblasts. Inhibition was complete at equimolar concentrations of IGF-I and bIGFBP-3. Inhibition of IGF-I-stimulated [3H]AIB uptake paralleled the ability of bIGFBP-3 to prevent [125I]IGF-I cell surface binding. In contrast, preincubation with bIGFBP-3 resulted in a dose-dependent enhancement of IGF-I-stimulated [3H]AIB uptake; a 32-86% increase in IGF-I bioactivity was seen after a 24 h preexposure to 10 nM bIGFBP-3, and a 2- to 6-fold potentiation was seen after a 72 h preincubation. Preincubation with bIGFBP-3 increased both the sensitivity and maximal responsiveness of the cells to IGF-I. The potentiating effects of bIGFBP-3 were associated with increased [125I]IGF-I binding to cultured bovine fibroblasts. Affinity cross-linking experiments indicated that the increase in IGF-I binding was due to increased membrane-associated bIGFBP-3 rather than to a bIGFBP-3-induced increase in type I IGF receptors. bIGFBP-3 had no effect on insulin stimulation of [3H]AIB uptake under either experimental condition. These data suggest that soluble bIGFBP-3 inhibits IGF-I action by sequestering and preventing IGF-I receptor binding, whereas surface-associated bIGFBP-3 enhances the growth-promoting effects of IGF-I in bovine fibroblasts. We propose that IGFBP-3 serves a dual function in modulating IGF action in vivo.
165 citations
TL;DR: The fluorescence spectra revealed that CPF causes the quenching of the fluorescence emission of serum albumin, and the alterations of protein secondary structure in the presence of CPF were confirmed by the evidences from UV and CD spectra.
Abstract: Chlorpyrifos (CPF) is a widely used organophosphate insecticide which could bind with human serum albumin (HSA) and bovine serum albumin (BSA). The binding behavior was studied employing fluorescence, three-dimensional fluorescence, Circular dichroism (CD) spectroscopy, UV-vis absorption spectroscopy, electrochemistry and molecular modeling methods. The fluorescence spectra revealed that CPF causes the quenching of the fluorescence emission of serum albumin. Stern-Volmer plots were made and quenching constants were thus obtained. The results suggested the formation of the complexes of CPF with serum albumins, which were in good agreement with the results from electrochemical experiments. Association constants at 25°C were 3.039 × 10(5) mol L(-1) for HSA, and 0.3307 × 10(5) mol L(-1) for BSA, which could affect the distribution, metabolism, and excretion of pesticide. The alterations of protein secondary structure in the presence of CPF were confirmed by the evidences from UV and CD spectra. Site competitive experiments also suggested that the primary binding site for CPF on serum albumin is close to tryptophan residues 214 of HSA and 212 of BSA, which was further confirmed by molecular modeling.
165 citations
TL;DR: Nano-crystalline Zn-containing hydroxyapatite (ZnHAp) was prepared by the wet-chemical method and the selective adsorption of essential proteins was examined, taking bovine serum albumin and pathogenic protein such as beta(2)-microglobulin (beta( 2)-MG) as model proteins.
165 citations
TL;DR: The conformational change in BSA at its native form after conjugation with GNPs confirmed that protein undergoes a more flexible conformational state on the boundary surface of GNPs after bioconjugation.
Abstract: Gold nanoparticles (GNPs) conjugated with biomolecules are promising building blocks for assembly into nanostructured functional materials for developing biomarker platforms because of their size dependent optical and electrical properties. Biocompatible GNPs were synthesized using glutamic acid as a reducing agent and the interaction between bovine serum albumin (BSA) and GNPs was investigated using fluorescence and circular dichroism (CD) spectroscopies. The binding constant (Kb) of protein (BSA) to GNPs was determined by measuring the quenching of the fluorescence intensity of tryptophan residues of the protein molecules after conjugation. The conformational change in BSA at its native form after conjugation with GNPs confirmed that protein undergoes a more flexible conformational state on the boundary surface of GNPs after bioconjugation. The CD studies further showed a decrease in the α-helical content after conjugation. The results confirmed that the change in conformation was larger at higher conce...
165 citations