scholarly journals Studies on the interaction between human serum protein fractions and 18O-labeled oxosteroids.

1988 ◽  
Vol 263 (6) ◽  
pp. 2824-2829
Author(s):  
C G Eriksson ◽  
P Eneroth
1965 ◽  
Vol 12 (6) ◽  
pp. 631-638 ◽  
Author(s):  
R.L. Searcy ◽  
S. Hayashi ◽  
E.M. Hardy ◽  
J.E. Berk

2021 ◽  
pp. 174751982199306
Author(s):  
Ya Gan ◽  
Ning Bai ◽  
Xitong Li ◽  
Shuiting Gao ◽  
Ruiyong Wang

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.


1970 ◽  
Vol 118 (5) ◽  
pp. 869-873 ◽  
Author(s):  
T. Freeman ◽  
J. Smith

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.


2006 ◽  
Vol 27 (17) ◽  
pp. 3410-3419 ◽  
Author(s):  
María A. Martínez-Gómez ◽  
Salvador Sagrado ◽  
Rosa M. Villanueva-Camañas ◽  
Maria J. Medina-Hernández

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