One-Step Purification of a Fusion Protein of Glucagon-Like Peptide-1 and Human Serum Albumin Expressed inPichia pastorisby an Immunomagnetic Separation Technique

2007 ◽  
Vol 71 (11) ◽  
pp. 2655-2662 ◽  
Author(s):  
Jiaqi CHEN ◽  
Gang BAI ◽  
Yu CAO ◽  
Zhihui GAO ◽  
Qi ZHANG ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Fusion Protein ◽  
Serum Albumin ◽  
Human Serum ◽  
Immunomagnetic Separation ◽  
Separation Technique ◽  
One Step ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1

scholarly journals Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide

2018 ◽  
Vol 293 (13) ◽  
pp. 4778-4791 ◽  
Author(s):  
Angélique Gajahi Soudahome ◽  
Aurélie Catan ◽  
Pierre Giraud ◽  
Sandrine Assouan Kouao ◽  
Alexis Guerin-Dubourg ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Glucagon Like Peptide ◽  
Glucagon Like Peptide 1

Long-Acting Human Serum Albumin-Thioredoxin Fusion Protein Suppresses Bleomycin-Induced Pulmonary Fibrosis Progression

2013 ◽  
Vol 345 (2) ◽  
pp. 271-283 ◽  
Author(s):  
Ryota Tanaka ◽  
Hiroshi Watanabe ◽  
Azusa Kodama ◽  
Victor Tuan Giam Chuang ◽  
Yu Ishima ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Pulmonary Fibrosis ◽  
Fusion Protein ◽  
Serum Albumin ◽  
Human Serum ◽  
Fibrosis Progression ◽  
Long Acting

Bioengineered Human Serum Albumin Fusion Protein as Target/Enzyme/pH Three-Stage Propulsive Drug Vehicle for Tumor Therapy

ACS Nano ◽  
2020 ◽  
Vol 14 (12) ◽  
pp. 17405-17418
Author(s):  
Mingyu Wang ◽  
Li Zhang ◽  
Yanfei Cai ◽  
Yang Yang ◽  
Lipeng Qiu ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Fusion Protein ◽  
Serum Albumin ◽  
Human Serum ◽  
Tumor Therapy ◽  
Drug Vehicle ◽  
Target Enzyme

scholarly journals TIMP-2 Fusion Protein with Human Serum Albumin Potentiates Anti-Angiogenesis-Mediated Inhibition of Tumor Growth by Suppressing MMP-2 Expression

PLoS ONE ◽  
2012 ◽  
Vol 7 (4) ◽  
pp. e35710 ◽  
Author(s):  
Mi-Sook Lee ◽  
Jae-In Jung ◽  
Seung-Hae Kwon ◽  
Sang-Mok Lee ◽  
Kyoji Morita ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Fusion Protein ◽  
Tumor Growth ◽  
Serum Albumin ◽  
Human Serum ◽  
Inhibition Of Tumor Growth

scholarly journals One-Step Preparation of Antifouling Polysulfone Ultrafiltration Membranes via Modification by a Cationic Polyelectrolyte Based on Polyacrylamide

Polymers ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 1017 ◽  
Author(s):  
Tatiana V. Plisko ◽  
Alexandr V. Bildyukevich ◽  
Katsiaryna S. Burts ◽  
Sergey S. Ermakov ◽  
Anastasia V. Penkova ◽  
...  
Keyword(s):  
Phase Separation ◽  
Human Serum Albumin ◽  
Zeta Potential ◽  
Serum Albumin ◽  
Human Serum ◽  
Cationic Polyelectrolyte ◽  
Coagulation Bath ◽  
Ultrafiltration Membranes ◽  
Selective Layer ◽  
One Step

A novel method for one-step preparation of antifouling ultrafiltration membranes via a non-solvent induced phase separation (NIPS) technique is proposed. It involves using aqueous 0.05–0.3 wt.% solutions of cationic polyelectrolyte based on a copolymer of acrylamide and 2-acryloxyethyltrimethylammonium chloride (Praestol 859) as a coagulant in NIPS. A systematic study of the effect of the cationic polyelectrolyte addition to the coagulant on the structure, performance and antifouling stability of polysulfone membranes was carried out. The methods for membrane characterization involved scanning electron microscopy (SEM), atomic force microscopy (AFM), Fourier transform infrared spectroscopy (FTIR), contact angle and zeta-potential measurements and evaluation of the permeability, rejection and antifouling performance in human serum albumin solution and surface water ultrafiltration. It was revealed that in the presence of cationic polyelectrolyte in the coagulation bath, its concentration has a major influence on the rate of “solvent–non-solvent” exchange and thus also on the rate of phase separation which significantly affects membrane structure. The immobilization of cationic polyelectrolyte macromolecules into the selective layer was confirmed by FTIR spectroscopy. It was revealed that polyelectrolyte macromolecules predominately immobilize on the surface of the selective layer and not on the bottom layer. Membrane modification was found to improve the hydrophilicity of the selective layer, to increase surface roughness and to change zeta-potential which yields the substantial improvement of membrane antifouling stability toward natural organic matter and human serum albumin.

scholarly journals Photoactivated covalent binding of [3H]bilirubin to human serum albumin

1979 ◽  
Vol 181 (3) ◽  
pp. 779-781 ◽  
Author(s):  
D W Hutchinson ◽  
D S Mutopo
Keyword(s):  
Aqueous Solution ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Good Yield ◽  
Covalent Binding ◽  
Covalent Attachment ◽  
Step Procedure ◽  
One Step ◽  
Degradation Studies

A one-step procedure has been developed for the preparation of [3H]bilirubin IX-alpha in good yield from unlabelled bilirubin. Irradiation of an aqueous solution of [3H]bilirubin IX-alpha in the presence of human serum albumin results in the covalent attachment of the bilirubin to the protein. Preliminary degradation studies have been carried out to locate the site of attachment of the bilirubin to the albumin.

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