Results 11 to 20 of about 638,695 (288)

Binding of anandamide to bovine serum albumin [PDF]

open access: yesJournal of Lipid Research, 2003
The endocannabinoid anandamide is of lipid nature and may thus bind to albumin in the vascular system, as do fatty acids. The knowledge of the free water-phase concentration of anandamide is essential for the investigations of its transfer from the ...
Inge N. Bojesen, Harald S. Hansen
doaj   +5 more sources

Bovine Serum Albumin Interactions with Metal Complexes [PDF]

open access: yesMedicine and Pharmacy Reports, 2014
The continuous search for new molecules with therapeutic abilities has led to the synthesis and characterization of a large number of metal complexes, proven to exhibit potential as pharmacological agents through their antibacterial, antiviral ...
T. Topală   +3 more
semanticscholar   +4 more sources

Noncovalent Interaction of Tilmicosin with Bovine Serum Albumin [PDF]

open access: yesMolecules, 2018
Tilmicosin is a widely used antibiotic in veterinary applications. Its antimicrobial activity is ranged from Gram-positive and some Gram-negative bacteria towards activities against Mycoplasma and Chlamydia.
Beáta Lemli   +4 more
doaj   +4 more sources

On the aggregation of bovine serum albumin

open access: yesJournal of Molecular Liquids, 2022
Abstract In an attempt to elucidate the aggregation behaviour of bovine serum albumin and its modulation by salt ions, size-exclusion high-performance liquid chromatography was used and complemented by dynamic light scattering. The influence of the protein concentration, and type and concentration of inorganic salt on the aggregation of albumin in ...
Madeira, Pedro P.   +4 more
openaire   +3 more sources

Interactions of tuftsin with bovine serum albumin [PDF]

open access: yesFEBS Letters, 1986
Interactions of tuftsin (Thr‐Lys‐Pro‐Arg) with bovine serum albumin (BSA) were analysed by fluorescence spectroscopy and circular dichroism. The data show that tuftsin interacts weakly with BSA, but this interaction is considerably enhanced by introducing an apolar substituent at the C‐terminus of the tetrapeptide.
Chhitar M. Gupta, Vinod Bhakuni
openaire   +3 more sources

Thermal coagulation of bovine serum albumin. [PDF]

open access: yesAgricultural and Biological Chemistry, 1981
The effects of salts were investigated on thermo-coagulation of bovine serum albumin (BSA). Salts affected the formation of coagulum, and a “minimum” (a col) on the turbidity-pH curve was observed at about pH 7.5. When the time course of turbidity was measured at more acidic pH (6.5) or alkaline pH (9.5), an induction period was observed at the more ...
Setsuro Matsushita, Kazuko Shimada
openaire   +3 more sources

The Aminopropylation of Bovine Serum Albumin [PDF]

open access: yesAustralian Journal of Biological Sciences, 1967
After the reaction of reduced BSAt with BPA at pH 10 6 and subsequent hydrolysis of the protein with 6N HCl, only 40% of the lysine present in the unmodified protein can be accounted for on chromatographic analysis of the hydrolysate; a similar loss is observed of the SAPC into which the original cystine, which has totally disappeared, is presumably ...
openaire   +3 more sources

Inducing the formation of a colloidal albumin carrier of curcumin

open access: yesJCIS Open, 2022
The administration and delivery of pharmaceuticals faces a variety of well-known obstacles that result in limited biocompatibility and bioavailability. Efforts to improve these properties have often employed serum albumin, primarily due to its inherent ...
Konstantina Matskou   +6 more
doaj  

Serum albumin binding knob domains engineered within a VH framework III bispecific antibody format and as chimeric peptides

open access: yesFrontiers in Immunology, 2023
BackgroundSerum albumin binding is an established mechanism to extend the serum half-life of antibody fragments and peptides. The cysteine rich knob domains, isolated from bovine antibody ultralong CDRH3, are the smallest single chain antibody fragments ...
Ralph Adams   +18 more
doaj   +1 more source

ATP binding to bovine serum albumin

open access: yesFEBS Letters, 1992
Specific binding or ATP to bovine serum albumin (BSA) is demonstrated employing ATP derivatives spin‐labeled at either N6 or C8 of adenine ring or at the ribose moiety. Based on a 1:1 stoichiometry binding constants are in the 50–100 μM range. Binding is largely competitive with ATP or stearic acid. A small fraction of the labeled nucleotides could not
Joachim Baumann   +2 more
openaire   +2 more sources

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