Effects of Temperature on Serum Protein Components in the Killifish, Fundulus heteroclitus

1970 ◽  
Vol 27 (2) ◽  
pp. 404-409 ◽  
Author(s):  
Bruce L. Umminger
Keyword(s):  
Immune Response ◽  
Cellulose Acetate ◽  
Serum Protein ◽  
Fundulus Heteroclitus ◽  
Serum Proteins ◽  
High Mobility ◽  
Electrophoretic Patterns ◽  
Effects Of Temperature ◽  
Protein Components ◽  
Microzone Electrophoresis

Electrophoretic patterns of serum proteins were studied in Fundulus heteroclitus acclimated to temperatures from 30 to −1.5 C. Microzone electrophoresis on cellulose acetate revealed eight distinct zones (seven anodal and one cathodal to the origin) at all temperatures. These zones were grouped into three larger zones (I, II, and III) for convenience in analysis. Low mobility proteins of zone III decreased in the cold to a greater degree than did high mobility proteins of zones II and I. The greater reduction in these low mobility proteins, which are comparable to human gamma globulins, might produce a less active immune response in cold-acclimated killifish.

Imprecision of quantification of serum protein fractions by electrophoresis on cellulose acetate.

1986 ◽  
Vol 32 (2) ◽  
pp. 356-357 ◽  
Author(s):  
S N Kahn ◽  
L P Strony
Keyword(s):  
High Resolution ◽  
Serum Albumin ◽  
Cellulose Acetate ◽  
Serum Protein ◽  
Protein Fractions ◽  
Visual Interpretation ◽  
Cellulose Acetate Electrophoresis ◽  
Trained Observer ◽  
Electrophoretic Patterns

Abstract We studied the precision of densitometric quantification of the protein zones resolved by cellulose acetate electrophoresis. Replicate analyses of patients' samples by a single technologist showed mean CVs ranging from 2.9% for serum albumin to 9.5% for alpha 1-globulin. There were marked differences in measurements obtained by replicate analysis of the same samples by two experienced technologists. We calculated what changes in fractional concentrations would be analytically significant and concluded that densitometry of cellulose acetate electrophoretograms can only be semi-quantitative. We suggest that visual interpretation of high-resolution electrophoretic patterns by a trained observer can replace densitometry in most cases.

Evaluation of a Cellulose-Acetate Electrophoresis System for Serum Protein Fractionation

1965 ◽  
Vol 11 (10) ◽  
pp. 937-942 ◽  
Author(s):  
Alex Kaplan ◽  
John Savory
Keyword(s):  
Cellulose Acetate ◽  
Serum Protein ◽  
Blood Donors ◽  
Serum Proteins ◽  
Normal Values ◽  
Protein Fractionation ◽  
Cellulose Acetate Electrophoresis ◽  
Cellulose Acetate Membranes ◽  
Control Serum ◽  
Electrophoresis System

Abstract A rapid system for the quantitative fractionation of serum proteins by electrophoresis on cellulose-acetate membranes was evaluated and found to be quite precise. The reproducibility (coefficient of variation) of the routine fractionation of a control serum carried out 40 times during a 15-week period was 2.4% for albumin and 14.2, 6.0, 6.1, and 5.2%, respectively, for the α1-, α2-, β-, and γ-globulin fractions. Normal values are given for serum protein fractions (specimens from nonprofessional blood donors) obtained by cellulose acetate electrophoresis.

Estimation of Serum Proteins by Electrophoresis on Cellulose Acetate

1972 ◽  
Vol 18 (12) ◽  
pp. 1541-1542 ◽  
Author(s):  
J W Keyser ◽  
G L Watkins
Keyword(s):  
Cellulose Acetate ◽  
Serum Protein ◽  
Serum Proteins ◽  
Standard Procedure ◽  
Total Serum Protein ◽  
Total Serum ◽  
Cellulose Acetate Electrophoresis ◽  
Ponceau S ◽  
Reference Serum ◽  
Electrophoresis Of Proteins

Abstract We have evaluated results for albumin obtained by a standard procedure for cellulose acetate electrophoresis of proteins in serum. The Ponceau S-stained albumin and globulins were eluted and the albumin was calculated by the generally accepted formula [(albumin-bound dye absorbance/absorbance of total protein-bound dye) x total serum protein concn] and by the formula (absorbance of albumin-bound dye in test/absorbance of albumin-bound dye in a reference serum) x concn of albumin in reference serum. The ratio of values by the first and second methods ranged from 0.93 to 1.30, the first giving the higher results in cases of discrepancy. These findings confirm the limitations in accurately calculating any serum-protein fraction by the first method. The second method appears to be the more accurate.

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.

Pathological changes associated with Oesophagostomum columbianum infestations in sheep: Serum protein changes after first infestation

1967 ◽  
Vol 18 (5) ◽  
pp. 821 ◽  
Author(s):  
C Dobson
Keyword(s):  
Cellulose Acetate ◽  
Serum Protein ◽  
Alimentary Tract ◽  
Serum Proteins ◽  
Immunological Response ◽  
Total Serum ◽  
Pathological Changes ◽  
Cellulose Acetate Electrophoresis ◽  
Globulin Level ◽  
Oesophagostomum Columbianum

The serum proteins of worm-free crossbred lambs were found to vary over a period of 10 weeks. Infestation of these lambs with 2000 infective Oesophagostomum columbianum larvae also caused marked changes in various serum proteins separated by cellulose acetate electrophoresis. The total serum proteins of infested sheep remained static or decreased slightly over the period of observation. There was a marked hypoalbuminaemia (measured in grams per cent.) in the infested lambs. The α-globulin retained the same level as in the controls; this was attributed to compensatory synthesis to overcome the osmotic changes produced by albumin loss. The ß1-globulin decreased throughout infestations; both albumin and ß1-globulin could have been lost through inflammation of the alimentary tract. The ß2-globulin increased very greatly during infestation; this was attributed to an immunological response. The y-globulin level at first decreased, but after 10 days the level increased at a rate commensurate with that in the control lambs. This increase was also attributed to an immunological response.

Electrophoresis of serum protein to detect alpha 1-antitrypsin deficiency: five illustrative cases.

1985 ◽  
Vol 31 (8) ◽  
pp. 1397-1399 ◽  
Author(s):  
R Malfait ◽  
F Gorus ◽  
C Sevens
Keyword(s):  
Serum Protein ◽  
Visual Inspection ◽  
Serum Proteins ◽  
Electrophoretic Pattern ◽  
The Other ◽  
Electrophoretic Patterns ◽  
Antitrypsin Deficiency ◽  
Alpha 1 Antitrypsin Deficiency ◽  
Alpha 1 Antitrypsin

Abstract We describe five cases of severe alpha 1-antitrypsin (AAT) deficiency to illustrate the importance of visual inspection of electrophoretic patterns of serum proteins. In four patients the diagnosis of AAT deficiency was clinically unsuspected; in the other patient, the electrophoretic pattern was the first clue to confirm the diagnosis. Densitometric scanning of these patterns invariably overestimated the concentration of alpha 1-globulin. By visually inspecting electrophoretic strips instead of relying on densitometry, clinical chemists can help detect AAT deficiency earlier.

scholarly journals Canine Serum Protein Responses to X-Irradiation

1984 ◽  
Vol 3 (4) ◽  
pp. 317-321
Author(s):  
H. J. Esber ◽  
P. Zavorskas ◽  
H. Rosenkrantz
Keyword(s):  
Lymph Nodes ◽  
Cellulose Acetate ◽  
Radiation Damage ◽  
Serum Protein ◽  
Plasma Protein ◽  
Immunoglobulin G ◽  
Inflammatory Process ◽  
Serum Proteins ◽  
Cellulose Acetate Electrophoresis ◽  
X Irradiation

It was of interest, in the absence of such data, to investigate the effects of x-irradiation on individual serum proteins, including immunoglobulin G. Doses of 600 and 800 rads to the abdominal areas of immature beagles were sufficient to evoke emesis and hemorrhages of lymph nodes and perilobular areas of the liver. Seven days after irradiation of 8–12 male dogs/dose, serum specimens were analyzed by cellulose acetate electrophoresis and radial immunodiffusion. Radiation reduced serum protein and albumin by 12%, β2 by 27%, γ-globulin by 19%, and IgG by 35%, while increasing α2 by 50%. These results are in conformity with the radiation damage to lymph nodes (IgG decrease) and liver (plasma protein fall) and initiation of the inflammatory process (α2 rise).

scholarly journals AN ELECTROPHORETIC STUDY ON SERUM PROTEINS IN ARABIAN RACE HORSES NATURALLY INFECTED WITH Babesia equi

2022 ◽  
Vol 21 (1) ◽  
pp. 1-13
Author(s):  
A.SH. SULTAN
Keyword(s):  
Serum Protein ◽  
Serum Proteins ◽  
Total Serum Protein ◽  
Total Serum ◽  
Electrophoretic Study ◽  
Babesia Equi ◽  
Electrophoretic Patterns ◽  
Race Horses

 Electrophoretic patterns of serum protein in 12 Arabian race horses acutely infected with Babesia equi revealed a significant decrease in albumin (P<0.01) and beta globulins (P<0.05) where, alpha globulins fractions significantly (P<0.01) increased. No significant (P>0.05) changes were recorded in gamma globulins fractions and total serum protein.

Two new non-barbiturate buffers for electrophoresis of serum proteins on cellulose acetate membranes.

1980 ◽  
Vol 26 (8) ◽  
pp. 1221-1223 ◽  
Author(s):  
J Ambler ◽  
M Rodgers
Keyword(s):  
Sodium Chloride ◽  
Cellulose Acetate ◽  
Serum Protein ◽  
Drugs Of Abuse ◽  
Sodium Salicylate ◽  
Serum Proteins ◽  
Protein Electrophoresis ◽  
The Other ◽  
Serum Protein Electrophoresis ◽  
Cellulose Acetate Membranes

Abstract Two new non-barbiturate buffers have been formulated for serum protein electrophoresis on cellulose acetate membranes. Both buffers give five distrinct fractions and are suitable for all systems, but have been primarily designed to meet the needs of the Gelman "Sepratek" system. One buffer is a tris(hydroxymethyl)aminomethane (Tris)/hippurate formulation; the other is composed of Tris/N-[tris(hydroxymethyl)methyl]glycine (Tricine)/sodium chloride/sodium salicylate. Both buffers allow reliable quantitation of protein fractions, giving results that correlated well with those obtained from barbiturate separations. The major advantage of these buffers is that they do not contain drugs of abuse.

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