scholarly journals Human serum protein fractionation by gel filtration

1970 ◽  
Vol 118 (5) ◽  
pp. 869-873 ◽  
Author(s):  
T. Freeman ◽  
J. Smith
Keyword(s):  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Gel Filtration ◽  
Protein Fractionation ◽  
Logical Approach ◽  
Complex Protein ◽  
Human Serum Protein ◽  
Immunological Technique ◽  
Current Terminology

The development of a quantitative immunological technique using polyvalent antiserum permits a more logical approach to the fractionation of complex protein mixtures. In this study whole serum was separated by conventional gel filtration and the fractions obtained were analysed. This demonstrates over 60 immunologically distinct serum proteins. Because the current terminology is inadequate to describe this number of proteins, a temporary numerical nomenclature has been used.

scholarly journals A study of the binding between radicicol and four proteins by means of spectroscopy and molecular docking

2021 ◽  
pp. 174751982199306
Author(s):  
Ya Gan ◽  
Ning Bai ◽  
Xitong Li ◽  
Shuiting Gao ◽  
Ruiyong Wang
Keyword(s):  
Molecular Docking ◽  
Human Serum ◽  
Serum Protein ◽  
Binding Constant ◽  
Inhibitory Effect ◽  
Experimental Results ◽  
Static Quenching ◽  
Spectroscopic Techniques ◽  
Quenching Process ◽  
Human Serum Protein

The interactions between radicicol and four proteins (catalase, trypsin, pepsin, and human serum protein) are investigated by spectroscopic techniques and molecular docking. A static quenching process is confirmed. The binding constant value between radicicol and human serum protein is the largest among the four proteins. Results reveal changes in the micro-environment of the protein by the addition of radicicol. It is found that radicicol shows an inhibitory effect on the activity of proteins (catalase, trypsin, and pepsin). Molecular docking results are consistent with the thermodynamic experimental results. This work provides clues to the elucidation of the mechanisms of the interactions between radicicol and proteins.

Characterization of basic drug–human serum protein interactions by capillary electrophoresis

2006 ◽  
Vol 27 (17) ◽  
pp. 3410-3419 ◽  
Author(s):  
María A. Martínez-Gómez ◽  
Salvador Sagrado ◽  
Rosa M. Villanueva-Camañas ◽  
Maria J. Medina-Hernández
Keyword(s):  
Capillary Electrophoresis ◽  
Human Serum ◽  
Serum Protein ◽  
Protein Interactions ◽  
Basic Drug ◽  
Human Serum Protein

scholarly journals Binding of Catecholamine with Human Serum Protein

1972 ◽  
Vol 22 ◽  
pp. 36
Author(s):  
Tadao Itoh ◽  
Masayo Yoshida ◽  
Kazuo Sawami ◽  
Yukiharu Inui ◽  
Shigeru Yoshida
Keyword(s):  
Human Serum ◽  
Serum Protein ◽  
Human Serum Protein

Separation of human serum proteins by high-speed gel filtration on TSK-GEL G3000SWG

1980 ◽  
Vol 3 (3) ◽  
pp. 145-145 ◽  
Author(s):  
Y. Kato ◽  
K. Komiya ◽  
H. Sasaki ◽  
T. Hashimoto
Keyword(s):  
Human Serum ◽  
High Speed ◽  
Serum Proteins ◽  
Gel Filtration ◽  
Human Serum Proteins

Human Saliva and Semen: Evidence for Proteins Common to Both Which Do Not Occur in Serum

1981 ◽  
Vol 60 (2) ◽  
pp. 179-184 ◽  
Author(s):  
P. D. Eckersall ◽  
J. A. Beeley
Keyword(s):  
Antibacterial Activity ◽  
Affinity Chromatography ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Rabbit Antiserum ◽  
Human Saliva ◽  
Cross Reactions ◽  
Whole Saliva ◽  
The Cross

1. Rabbit antiserum to human whole saliva cross-reacts with both human serum and semen. After absorption of the antiserum by affinity chromatography on a column of immobilized serum protein, the cross-reactions with serum were eliminated. 2. The absorbed antiserum, however, still cross-reacted with semen thus indicating the presence of proteins with immunological similarity in both saliva and semen, but which did not occur in serum. 3. Some of these proteins clearly showed a reaction of complete immunological identity between saliva and semen. 4. The presence of the non-serum proteins in both saliva and semen might be related to common functions in both such as lubrication or antibacterial activity.

Sign in / Sign up

Export Citation Format

Share Document