Results 221 to 230 of about 468,755 (304)
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The cryoaggregation of bovine serum albumin

Cryobiology, 1970
Summary Bovine serum albumin in the native (BSA), reduced (BSA-SH), and combined (BSA-S-NEM) forms was frozen at −5°C. The BSA remained essentially soluble; the BSA-SH and BSA-S-NEM both aggregated nearly completely when allowed to reimbibe water at room temperature but to a smaller degree when allowed to reimbibe just above the freezing point.
R, Goodin, J, Levitt
openaire   +2 more sources

Antigenic Determinants of Bovine Serum Albumin

International Archives of Allergy and Immunology, 2001
<i>Background:</i> Bovine serum albumin (BSA) is one of the most widely studied proteins; its structure is well known and its antigenic characteristics have been described in several papers. The aim of this research was the identification of the BSA antigenic determinants.
Beretta B   +10 more
openaire   +2 more sources

Bovine Serum Albumin as a Versatile Platform for Cancer Imaging and Therapy.

Current Medicinal Chemistry, 2018
BACKGROUND Due to the good biocompatibility, biodegradability, facile surface functionalization and high water solubility, Bovine serum albumin has gain increasing attention in the nanomedicine. OBJECTIVE Despite there are many reviews on albumin based
Jun Wang, Bingbo Zhang
semanticscholar   +1 more source

Investigation on the conformational changes of bovine serum albumin in a wide pH range from 2 to 12

Spectroscopy Letters, 2018
The conformation of bovine serum albumin largely depends on its microenvironment pH and affects its physical functions and applications. In this study, we investigated the effects of pH (wide range 2–12) on the conformation of bovine serum albumin based ...
Zhenxing Chi   +5 more
semanticscholar   +1 more source

Binding of isofraxidin to bovine serum albumin

Biopolymers, 2004
AbstractThe binding of isofraxidin to bovine serum albumin (BSA) was studied under physiological conditions with BSA concentration of 1.5×10−6 mol · L−1 and drug concentration in the range of 1.67×10−6 mol · L−1 to 2.0×10−5 mol · L−1. Fluorescence quenching spectra in combination with uv absorption spectroscopy, Fourier transform infrared (FTIR ...
Jiaqin, Liu   +3 more
openaire   +2 more sources

The binding of mercury to bovine serum albumin

Environmental Research, 1973
Abstract Additional studies on the binding of mercury by serum albumin is presented. Data were obtained by radiotracer methods and the technique of equilibrium dialysis. The results showed that mercury is bound at other sites in addition to the carboxyl and sulfydryl groups reported previously.
S A, Katz, M H, Samitz
openaire   +2 more sources

The heterogeneity of bovine serum albumin

Biochimica et Biophysica Acta (BBA) - General Subjects, 1966
Abstract 1. 1. The different components of native and modified bovine serum albumin have been investigated with respect to differences in composition and structure. It was found that native bovine serum albumin is composed of at least 3 components, and that most bovine serum albumin samples contain 4.
openaire   +2 more sources

Binding of naproxen to bovine serum albumin and tryptophan-modified bovine serum albumin

Proceedings / Indian Academy of Sciences, 1987
Two classes of binding sites, a single high-affinity site with an association constant of 4·8×106 M−1 and two low-affinity sites with association constant of about 0·05×106 M−1 have been observed in the interaction of Naproxen with bovine serum albumin (BSA).
Meenakshi Maruthamuthu, S Kishore
openaire   +1 more source

Conjugate of bovine serum albumin with nicotine

Biochemical and Biophysical Research Communications, 1974
Abstract The preparation and characterization of a nicotine-albumin conjugate are reported. The nicotine derivative, 6-(p-aminobenzamido)nicotine, which was coupled to bovine serum albumin(BSA), was synthesized by the following sequence; 1 -nicotine→6-aminonicotine→6-(p-nitrobenzamido)nicotine→6-(p-aminobenzamido)nicotine.
H, Matsushita, M, Noguchi, E, Tamaki
openaire   +2 more sources

Aggregation and fibrillation of bovine serum albumin

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2007
The all-alpha helix multi-domain protein bovine serum albumin (BSA) aggregates at elevated temperatures. Here we show that these thermal aggregates have amyloid properties. They bind the fibril-specific dyes Thioflavin T and Congo Red, show elongated although somewhat worm-like morphology and characteristic amyloid X-ray fiber diffraction peaks ...
Holm, NK   +9 more
openaire   +4 more sources

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