scholarly journals Comparative studies on the half-life of I131-labeled albumins and nonradioactive human serum albumin in a case of analbuminemia

1961 ◽  
Vol 40 (3) ◽  
pp. 475-475
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Comparative Studies ◽  
Half Life

Comparative studies of the serum half-life extension of a protein via site-specific conjugation to a species-matched or -mismatched albumin

2018 ◽  
Vol 6 (8) ◽  
pp. 2092-2100 ◽  
Author(s):  
Byungseop Yang ◽  
Jong Chul Kim ◽  
Jihyoun Seong ◽  
Giyoong Tae ◽  
Inchan Kwon
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Comparative Studies ◽  
Half Life ◽  
Therapeutic Proteins ◽  
Life Extension ◽  
Site Specific

Human serum albumin (HSA) has been investigated as a serum half-life extender of therapeutic proteins thanks to its unusually long serum half-life.

scholarly journals Rapid identification of Human Serum Albumin binding peptides from a phage display library：a back-of-the-envelope assessment of positive binders using titer-based criteria

2015 ◽  
Author(s):  
Yi-Feng Shi ◽  
Min Li ◽  
Jia-Di Zhang ◽  
Lei Bian
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Phage Display ◽  
Human Serum ◽  
Half Life ◽  
Drug Carrier ◽  
Therapeutic Proteins ◽  
Blood Protein ◽  
Albumin Binding ◽  
Binding Peptides

Human serum albumin (HSA) is the most abundant protein in blood and has a 19-day in vivo half-life, the longest human blood protein. HSA has also been extensively studied as a drug carrier in a wide variety of clinical applications. HSA-binding, compared with HSA-fusion, is promising strategy for extending the plasma half-life of protein therapeutics. The construction of albumin-binding drugs requires assessment of a large enough quantity of HSA-binding peptide candidates for conjugation with therapeutic proteins. Here, we report a back-of-the-envelope assessment method to facilitate phage display selection of HSA-binding peptides. With an experimentally determined number of phage titers, we can calculate the specificity ratios and the recovery yields. The recovery yield is calculated using the titers of eluted phage divided by the titers of input phage. The specificity ratio is calculated using the titer of eluted phage from a target-coated plate divided by the titer of eluted phage from a blank-control plate. These parameters are defined as quantitative criteria for panning and characterization of binding phage clones. Consequently, this approach may enable more rapid and low-cost phage display screening of HSA-binding peptides, which could be used as candidates of HSA binders for conjugation with therapeutic proteins.

scholarly journals Comparative Studies on the Human Serum Albumin Binding of the Investigational EGFR Inhibitor KP2187, Its Hypoxia-Activated Cobalt Complex, and a Series of Clinically Approved Inhibitors

Proceedings ◽  
2019 ◽  
Vol 22 (1) ◽  
pp. 27
Author(s):  
Eva Anna Enyedy ◽  
Orsolya Dömötör ◽  
Attila Borics ◽  
Bernhard K. Keppler ◽  
Christian R. Kowol
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Comparative Studies ◽  
Cobalt Complex ◽  
Albumin Binding ◽  
Egfr Inhibitor ◽  
Binding Interactions ◽  
Human Serum Albumin Binding

Binding interactions between human serum albumin and four clinically approved epidermal [...]

Temperature dependence of certain integrated membrane functions in macrophages

1982 ◽  
Vol 57 (1) ◽  
pp. 115-127
Author(s):  
M Faghihi Shirazi ◽  
N.N. Aronson ◽  
R.T. Dean
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Half Life ◽  
Bovine Serum ◽  
Fluid Phase ◽  
Peritoneal Macrophages ◽  
Turnover Time ◽  
Effect Of Temperature

We have studied the effect of temperature on uptake and degradation of molecules entering mouse peritoneal macrophages by fluid-phase, adsorptive and receptor-mediated pinocytosis, and on degradation of their intracellular proteins. Uptake of [3H]sucrose and uptake and degradation of formaldehyde-treated 125I-labelled human serum albumin and 125I-labelled mannose-bovine serum albumin continued, but were progressively slowed as the temperature decreased from 37 degrees C to 20 degrees C. The uptake and degradation were completely abolished at approximately 15 degrees C. Arrhenius plots for adsorptive and fluid uptake were unilinear, whereas that for receptor-mediated endocytosis showed an inflection point at approximately 20 degrees C. The results did not indicate any distinction between adsorptive and fluid pinocytosis. An ‘intracellular turnover time’ calculated for mannose-bovine serum albumin taken up by the specific route is 19–24 min and this time calculated for human serum albumin is, in contrast, 99 min. Studies of the kinetics of degradation of both endocytosed and endogenous proteins showed similarity in the temperature cut-off of degradation of endocytosed and endogenous long-half-life proteins (congruent to 15 degrees C) and continuance of endogenous short-half-life degradation at much lower temperatures.

scholarly journals Comparative Studies of Interactions between Fluorodihydroquinazolin Derivatives and Human Serum Albumin with Fluorescence Spectroscopy

Molecules ◽  
2016 ◽  
Vol 21 (10) ◽  
pp. 1373 ◽  
Author(s):  
Yi Wang ◽  
Meiqing Zhu ◽  
Feng Liu ◽  
Xiangwei Wu ◽  
Dandan Pan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Comparative Studies
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