The binding of thio-TEPA in human serum and to isolated serum protein fractions

1987 ◽  
Vol 20 (4) ◽  
Author(s):  
Bj�rn Hagen ◽  
OddG. Nilsen
Keyword(s):  
Human Serum ◽  
Serum Protein ◽  
Protein Fractions

Cystine in Human Serum Proteins

1956 ◽  
Vol 2 (2) ◽  
pp. 65-74 ◽  
Author(s):  
Miriam Reiner ◽  
Michael X Sullivan
Keyword(s):  
Multiple Myeloma ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Normal Serum ◽  
The Other ◽  
Protein Fractions ◽  
Human Hemoglobin ◽  
Average Value ◽  
Human Serum Proteins

Abstract 1. The amount of cystine was determined in a number of serum protein fractions separated by the procedure of E. J. Cohn. In albumin, the average value was 6.40 per cent for cystine; for γ-globulin the average value was 1.94 per cent; the other fractions tested were mixtures and varied according to the different globulins present. Globin from human hemoglobin contained 1.90 per cent cystine. 2. Separated fractions from three types of multiple myeloma cases have been presented showing abnormal fractions in the α-, β-, and γregions. The percentage of cystine was determined, and except for the fraction from the "gamma" type of myelomas, which contained 6.15 per cent cystine, the anomalous protein fractions contained about the same amount found in separated fractions of normal serum.

Measurement of Polarographically Active Sulfur in Human Serum Fractions Obtained by Paper Electrophoresis

1970 ◽  
Vol 16 (3) ◽  
pp. 155-157 ◽  
Author(s):  
Jiří Homolka
Keyword(s):  
Human Serum ◽  
Serum Protein ◽  
Paper Electrophoresis ◽  
Protein Fractions ◽  
X Ray ◽  
Serum Fractions

Abstract Polarographically active sulfur was distributed among the serum-protein fractions as follows (in percentages): albumin, 63.21; α1-globulin, 3.17; α2-globulin, 7.92; β-globulin, 14.54; α-globulin, 11.16. The results compare well with those obtained by X-ray spectrometry. The same method was applied to sera from patients suffering from malignant processes and some other diseases; the percentage of polarographically active sulfur in fractions of plasma from diseased individuals varied considerably.

The interaction of human serum protein fractions with the starch-iodine complex

1965 ◽  
Vol 12 (6) ◽  
pp. 631-638 ◽  
Author(s):  
R.L. Searcy ◽  
S. Hayashi ◽  
E.M. Hardy ◽  
J.E. Berk
Keyword(s):  
Human Serum ◽  
Serum Protein ◽  
Protein Fractions ◽  
Iodine Complex ◽  
Human Serum Protein

The alkaline reducing activity of glycated serum proteins and its relevance to diabetes mellitus.

1986 ◽  
Vol 32 (2) ◽  
pp. 368-370 ◽  
Author(s):  
R N Johnson ◽  
J R Baker
Keyword(s):  
Diabetes Mellitus ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Fractions ◽  
Glycated Protein ◽  
Reducing Activity

Abstract We investigated the ability of the fructosamine assay to detect glycation of serum proteins. We incubated both whole human serum and serum protein fractions in vitro with [14C]glucose, and analyzed for reducing activity and for uptake of 14C by protein. In all experiments, the reducing activity increased linearly with time for seven days and was correlated with 14C uptake (r = 0.94-0.98). Protein ketoamines were about fivefold more actively reducing than equimolar concentrations of deoxymorpholinofructose, the fructosamine standard, which explains why values for fructosamine in serum are higher than the expected concentration of protein ketoamines. We also used [14C, 2-3H]glucose to assess the contribution of the aldimine component to 14C uptake. Whole human serum and albumin incubated with [14C, 2-3H]glucose showed little uptake of 3H in relation to 14C. We conclude that glycated protein can be simply and reliably quantified by the fructosamine assay, and we discuss the relevance of this conclusion to the monitoring of diabetes.

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