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.

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 Studies in Bisalbuminemia: Binding Properties of the Two Albumins

Blood ◽  
1962 ◽  
Vol 20 (2) ◽  
pp. 156-164 ◽  
Author(s):  
EDWARD J. SARCIONE ◽  
C. WILLIAM AUNGST
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Total Serum ◽  
Binding Properties ◽  
Normal Human ◽  
Serum Components

Abstract 1. An abnormal serum protein pattern in a patient with Wegener’s granulomatosis and five of his relatives was identified as bisalbuminemia by electrophoretic and immunochemical methods. 2. With the exception of the patient with Wegener’s syndrome, the presence of bisalbuminemia was not associated with a significant change in total serum proteins, total albumin, serum components other than albumin, or any disease. 3. Addition of I131-thyroxine to bisalbumin sera resulted in thyroxine binding by albumin B but not by albumin A. The failure of albumin A to bind added I131-thyroxine leads to speculation that, in this family, neither albumin A nor B are identical to normal human serum albumin.

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.

scholarly journals The Impact of Graphite Oxide Nanocomposites on the Antibacterial Activity of Serum

2021 ◽  
Vol 22 (14) ◽  
pp. 7386
Author(s):  
Katarzyna Dorota Morka ◽  
Maciej Wernecki ◽  
Anna Kędziora ◽  
Marta Książczyk ◽  
Bartłomiej Dudek ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Human Serum ◽  
Complement System ◽  
Graphite Oxide ◽  
Galleria Mellonella ◽  
Serum Proteins ◽  
Normal Human Serum ◽  
Normal Human ◽  
The Impact ◽  
The Complement System

Nanoparticles can interact with the complement system and modulate the inflammatory response. The effect of these interactions on the complement activity strongly depends on physicochemical properties of nanoparticles. The interactions of silver nanoparticles with serum proteins (particularly with the complement system components) have the potential to significantly affect the antibacterial activity of serum, with serious implications for human health. The aim of the study was to assess the influence of graphite oxide (GO) nanocomposites (GO, GO-PcZr(Lys)2-Ag, GO-Ag, GO-PcZr(Lys)2) on the antibacterial activity of normal human serum (NHS), serum activity against bacteria isolated from alveoli treated with nanocomposites, and nanocomposite sensitivity of bacteria exposed to serum in vitro (using normal human serum). Additionally, the in vivo cytotoxic effect of the GO compounds was determined with application of a Galleria mellonella larvae model. GO-PcZr(Lys)2, without IR irradiation enhance the antimicrobial efficacy of the human serum. IR irradiation enhances bactericidal activity of serum in the case of the GO-PcZr(Lys)2-Ag sample. Bacteria exposed to nanocomposites become more sensitive to the action of serum. Bacteria exposed to serum become more sensitive to the GO-Ag sample. None of the tested GO nanocomposites displayed a cytotoxicity towards larvae.

scholarly journals Automated Multicapillary Electrophoresis for Analysis of Human Serum Proteins

2003 ◽  
Vol 49 (11) ◽  
pp. 1909-1915 ◽  
Author(s):  
Cécile Gay-Bellile ◽  
Djaouida Bengoufa ◽  
Pascal Houze ◽  
Didier Le Carrer ◽  
Mourad Benlakehal ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Protein ◽  
Serum Proteins ◽  
Protein Analysis ◽  
Fused Silica ◽  
Ease Of Use ◽  
Computer Assisted ◽  
Serum Samples ◽  
Bar Code ◽  
Electrophoretic Patterns

Abstract Background: We evaluated a new, automated multicapillary zone electrophoresis (CE) instrument (Capillarys®, 4.51 software version; Sebia) for human serum protein analysis. Methods: With the Capillarys β1-β2+® reagent set, proteins were separated at 7 kV for 4 min in 15.5 cm × 25 μm fused-silica capillaries (n = 8) at 35.5 °C in a pH 10 buffer with online detection at 200 nm. Serum samples with different electrophoretic patterns (n = 265) or potential interference (n = 69) were analyzed and compared with agarose gel electrophoresis (AGE; Hydrasys®-Hyrys®, Hydragel protein(e) 15/30® reagent set; Sebia). Results: CVs were <3.5% for albumin, <11% for α1-globulin, <4.1% for α2-globulin, <7.4% for β-globulin, and <5.8% for γ-globulin (3 control levels); measured throughput was 60 samples/h. In patients without paraprotein (n = 116), the median differences between CE and AGE were −5.4 g/L for albumin, 4.0 g/L for α1-globulin, 0.7 g/L for α2-globulin, 0.6 g/L for β-globulin (P <0.001 for all fractions), and −0.1 g/L for γ-globulin (not significant). More samples had at least one γ-migrating peak detected by CE (n = 135 vs 130; paraprotein detection limit, ∼0.5–0.7 g/L), but fewer were quantified (n = 84 vs 91) because of γ- to β-migration shifts. There was a 1.2 g/L median difference between CE and AGE for γ-migrating paraprotein quantification (n = 69; P <0.001). Several ultraviolet-absorbing substances (lipid emulsion, hemoglobin) or molecules (contrast agent, gelatin-based plasma substitute) induced CE artifacts. Conclusions:The Capillarys instrument is a reliable CE system for serum protein analysis, combining advantages of full automation (ease of use, bar-code identification, computer-assisted correction of α1-globulins) with high analytical performances and throughput.

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.

Sign in / Sign up

Export Citation Format

Share Document