Results 11 to 20 of about 1,302,182 (255)

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.
Bhakuni, Vinod, Gupta, C.M.
openaire   +3 more sources

SHEAR FLOW OF BOVINE SERUM ALBUMIN SOLUTIONS [PDF]

open access: yesStudia Universitatis Babes-Bolyai Chemia, 2019
In this paper, the flow of bovine serum albumin (BSA) solutions in physiological serum was investigated at different concentrations from 1 to 10 g/dL and temperatures from 4°C to 80°C.
Maria BERCEA   +3 more
doaj   +2 more sources

Allosteric modulation of zinc speciation by fatty acids [PDF]

open access: yes, 2013
Background: Serum albumin is the major protein component of blood plasma and is responsible for the circulatory transport of a range of small molecules that include fatty acids, hormones, metal ions and drugs.
Barnett, James P.   +10 more
core   +2 more sources

Bovine Serum Albumin as A Superior “FP-Tag” for High-Throughput Glycosyltransferase Assay [PDF]

open access: yes, 2020
Here, we report the development of a high-throughput “FP-Tag” OGT assay with bovine serum albumin as a low-cost and superior “FP-Tag”. With this assay, 2-methyleurotinone was identified as a low M-range OGT inhibitor.
Jiaxin, Li   +7 more
core   +1 more source

Allosteric inhibition of cobalt binding to albumin by fatty acids : implications for the detection of myocardial ischemia [PDF]

open access: yes, 2012
The biomarker "ischemia-modified albumin" (IMA), measured by the albumin-cobalt-binding assay (ACB assay), is the only FDA-approved biomarker for early diagnosis of myocardial ischemia.
Peter J. Sadler   +11 more
core   +1 more source

Translational and rotational motions of albumin sensed by a non-covalent associated porphyrin under physiological and acidic conditions: a fluorescence correlation spectroscopy and time resolved anisotropy study. [PDF]

open access: yes, 2008
The interaction between a free-base, anionic water-soluble porphyrin, TSPP, and the drug carrier protein, bovine serum albumin (BSA) has been studied by time-resolved fluorescence anisotropy (TRFA) and fluorescence correlation spectroscopy (FCS) at two ...
Costa, S.M.   +4 more
core   +1 more source

Glutaraldehyde-Polymerized Hemoglobin: In Search of Improved Performance as Oxygen Carrier in Hemorrhage Models

open access: yesBioinorganic Chemistry and Applications, 2020
Hemoglobin- (Hb-) based oxygen carriers (HBOC) have for several decades been explored for treatment of hemorrhage. In our previous top-up tests, HBOC with lower in vitro prooxidant reactivity (incorporating a peroxidase or serum albumin to this end ...
Anca D. Farcas   +5 more
doaj   +1 more source

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   +2 more sources

TALEN-mediated modification of the bovine genome for large-scale production of human serum albumin.

open access: yesPLoS ONE, 2014
As an initial step towards creating genetically modified cattle as a biopharming source of recombinant human serum albumin (rHSA), we report modification of the bovine albumin (bA) locus by transcription activator-like effector nuclease (TALEN ...
Shaida Moghaddassi   +2 more
doaj   +1 more source

Plasma free fatty acid levels influence Zn2+-dependent histidine-rich glycoprotein-heparin interactions via an allosteric switch on serum albumin [PDF]

open access: yes, 2014
Background: Histidine-rich glycoprotein (HRG) regulates coagulation, through its ability to bind and neutralize heparins. HRG associates with zinc ions (Zn2+) to stimulate HRG-heparin complex formation. Under normal conditions the majority of plasma Zn2+
Schwarz-Linek, Ulrich   +6 more
core   +1 more source

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