scholarly journals SP-40,40, a newly identified normal human serum protein found in the SC5b-9 complex of complement and in the immune deposits in glomerulonephritis.

1988 ◽  
Vol 81 (6) ◽  
pp. 1858-1864 ◽  
Author(s):  
B F Murphy ◽  
L Kirszbaum ◽  
I D Walker ◽  
A J d'Apice
Keyword(s):  
Human Serum ◽  
Serum Protein ◽  
Normal Human Serum ◽  
Immune Deposits ◽  
Human Serum Protein ◽  
Normal Human

Evaluation of a commercially available radioimmunoassay kit for measurement of doxorubicin in plasma.

1982 ◽  
Vol 28 (1) ◽  
pp. 119-121 ◽  
Author(s):  
E Piall ◽  
G W Aherne ◽  
V Marks
Keyword(s):  
Human Serum ◽  
Normal Human Serum ◽  
Nonspecific Effects ◽  
Normal Human ◽  
Doxorubicin Concentration

Abstract We evaluated a commercially available (Diagnostic Biochemistry Inc.) doxorubicin 125I radioimmunoassay kit. This kit gave a high apparent doxorubicin concentration (greater than 12 micrograms/L), which was not linearly related to dilution, for two pools of normal human serum and plasma and also for samples collected from patients before they received the drug. In contrast, a doxorubicin 3H radioimmunoassay developed by us gave a low blank (2 micrograms/L), which was linearly related to dilution, for the same pools and patients' samples. Doxorubicin concentrations in the plasma of patients receiving the drug were compared by the two methods; the kit gave results five- to 10-fold those obtained with our assay. High nonspecific interference by serum and plasma as measured by the 125I radioimmunoassay must therefore be borne in mind by users of the kit, and we suggest that results should be corrected for these nonspecific effects.

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.

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.

The Presence of Two Forms of Insulin in Normal Human Serum

Biochemistry ◽  
1963 ◽  
Vol 2 (2) ◽  
pp. 286-289 ◽  
Author(s):  
Walter N. Shaw ◽  
Eldon W. Shuey
Keyword(s):  
Human Serum ◽  
Normal Human Serum ◽  
Normal Human
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