Electrophoresis, Specific Protein Assays, or Both in Measurement of Plasma Proteins?

1973 ◽  
Vol 19 (1) ◽  
pp. 99-102 ◽  
Author(s):  
Carl Bertil Laurell
Keyword(s):  
Serum Protein ◽  
Plasma Proteins ◽  
Protein Composition ◽  
Relevant Information ◽  
Specific Protein ◽  
Electrophoretic Separation ◽  
Visual Evaluation ◽  
Specific Analysis ◽  
Cumulative Knowledge ◽  
Protein Assays

Abstract Cumulative knowledge of the protein composition of plasma and newer techniques for specific analysis of proteins have made obsolete most flocculation tests, the albumin:globulin ratio, scanning diagrams, and most determinations of electrophoretic fractions. More clinically relevant information about the serum protein composition is obtained by critical visual evaluation of the protein bands obtained after electrophoretic separation of plasma or serum in nonadsorptive supporting media, if supplementary specific analysis is made of a small number of proteins such as albumin, orosomucoid, haptoglobins, ceruloplasmin, and the immunoglobulins of the three predominant classes

Diagnostic Effectiveness of Electrophoresis and Specific Protein Assays, Evaluated by Discriminate Analysis

1972 ◽  
Vol 18 (2) ◽  
pp. 116-123 ◽  
Author(s):  
Mario Werner ◽  
Samuel H Brooks ◽  
Georg Cohnen
Keyword(s):  
Multivariate Analysis ◽  
Clinical Diagnosis ◽  
Serum Protein ◽  
Protein Pattern ◽  
Paper Electrophoresis ◽  
Specific Protein ◽  
Discriminate Analysis ◽  
Disease Discrimination ◽  
Protein Assays

Abstract With use of the serum protein pattern as a model, we compared the "Diagnostic Effectiveness" of tests of different chemical specificity—i.e., the percentage classified correctly according to the clinical diagnosis. When results obtained from a selected population of subjects with selected diseases were evaluated by multivariate analysis, disease discrimination by paper electrophoresis, which resolves only chemically heterogeneous fractions, was similar to that of a battery of specific assays for individual proteins.

Appropriate sera for calibration and control of specific protein assays

1993 ◽  
Vol 53 ◽  
pp. 13-15 ◽  
Author(s):  
O. Blaabjerg ◽  
M. Blom ◽  
H. Gry ◽  
P. Hyltoft Petersen ◽  
A. Uldall
Keyword(s):  
Specific Protein ◽  
And Control ◽  
Protein Assays

THE EFFECT OF REPEATED HEAT AND COLD EXPOSURE ON SERUM PROTEIN COMPOSITION IN MAN

1967 ◽  
Vol 45 (4) ◽  
pp. 571-575 ◽  
Author(s):  
W. F. Blatt ◽  
J. Kerkay
Keyword(s):  
Serum Protein ◽  
Cold Exposure ◽  
Total Protein ◽  
Protein Composition ◽  
Total Serum Protein ◽  
Total Serum ◽  
Heat Acclimatization ◽  
Albumin Content ◽  
Protein Serum ◽  
Lipoprotein Distribution

Total protein, serum protein, and lipoprotein electrophoretic distribution and hematocrit values were determined in two groups of men during acclimatization to 6 weeks of cold and 11 days of heat respectively. After 3 weeks of cold exposure total serum protein and albumin content decreased, while the globulin fractions increased; thus, the calculated albumin/globulin ratio was significantly depressed. During the last 2 weeks, these parameters gradually returned to control values. Overall, the protein changes during heat acclimatization were minimal, although the globulins decreased slightly, yielding a small increase in the albumin/globulin ratio. The hematocrit levels were significantly lowered during both environmental exposures, whereas the lipoprotein distribution remained essentially unchanged.

EFFECTS OF PORCINE IMMUNE GLOBULIN ADMINISTRATION ON THE SURVIVAL AND SERUM PROTEIN COMPOSITION OF COLOSTRUM-DEPRIVED PIGS REARED IN A NON-ISOLATED ENVIRONMENT

1961 ◽  
Vol 41 (2) ◽  
pp. 236-252 ◽  
Author(s):  
B. D. Owen ◽  
J. M. Bell ◽  
C. M. Williams ◽  
R. G. Oakes
Keyword(s):  
Oral Administration ◽  
Serum Protein ◽  
Immune Globulin ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Post Partum ◽  
Protein Composition ◽  
Paper Strip ◽  
Percentage Survival ◽  
Immune Globulins

Five experiments involving 90 newborn colostrum-deprived pigs were conducted in an attempt to develop a method of rearing applicable in a non-isolated environment. Immune globulins, prepared by ammonium sulphate fractionation of porcine serum, and comprised of a mixture of approximately 75 per cent γ-globulin and 25 per cent β-globulin, were administered orally or parenterally in varying amounts and for varying periods of time. In two experiments porcine albumin, in serum or in a semi-purified solution, was provided in addition to the immune globulins. The distribution of serum proteins in the pigs was studied from birth to 12 weeks of age by paper strip electrophoresis.Parenteral administration of immune globulins did not provide an effective passive immunity, nor did oral administration for 1 day post-partum. A marked improvement in survival occurred when oral administration was continued for 5 days, and it was further found that this treatment provided apparently complete protection against infection during the 5-day period of administration. Albumin appeared to further improve survival.These results, together with the relatively poor survival obtained with positive control pigs (nursed 24 hours) suggested a continuing need for a supply of immune globulins in the lumen of the intestinal tract. Presumably these globulins were active as coproantibodies.The percentage survival in pigs weighing 3 pounds or more at birth was substantially higher than in smaller pigs. Mortality in these experiments was usually attributable to colibacillosis.Serum immune globulin levels at 2 days of age in the artificially reared pigs were elevated in proportion to the amount of globulins given. The effect of albumin was to create a serum protein pattern resembling that of suckled pigs. A marked decline in γ-globulin levels from 2 days to approximately 6 weeks was observed.

scholarly journals The Ubiquitin-Proteasome System Does Not Regulate the Degradation of Porcine β-Microseminoprotein during Sperm Capacitation

2020 ◽  
Vol 21 (11) ◽  
pp. 4151
Author(s):  
Lucie Tumova ◽  
Michal Zigo ◽  
Peter Sutovsky ◽  
Marketa Sedmikova ◽  
Pavla Postlerova
Keyword(s):  
Seminal Plasma ◽  
Plasma Proteins ◽  
Protein Composition ◽  
Surface Protein ◽  
Ubiquitin Proteasome System ◽  
Sperm Capacitation ◽  
Sperm Surface ◽  
Ubiquitin Proteasome ◽  
Seminal Plasma Proteins

Sperm capacitation, one of the key events during successful fertilization, is associated with extensive structural and functional sperm remodeling, beginning with the modification of protein composition within the sperm plasma membrane. The ubiquitin-proteasome system (UPS), a multiprotein complex responsible for protein degradation and turnover, participates in capacitation events. Previous studies showed that capacitation-induced shedding of the seminal plasma proteins such as SPINK2, AQN1, and DQH from the sperm surface is regulated by UPS. Alterations in the sperm surface protein composition also relate to the porcine β-microseminoprotein (MSMB/PSP94), seminal plasma protein known as immunoglobulin-binding factor, and motility inhibitor. MSMB was detected in the acrosomal region as well as the flagellum of ejaculated boar spermatozoa, while the signal disappeared from the acrosomal region after in vitro capacitation (IVC). The involvement of UPS in the MSMB degradation during sperm IVC was studied using proteasomal interference and ubiquitin-activating enzyme (E1) inhibiting conditions by image-based flow cytometry and Western blot detection. Our results showed no accumulation of porcine MSMB either under proteasomal inhibition or under E1 inhibiting conditions. In addition, the immunoprecipitation study did not detect any ubiquitination of sperm MSMB nor was MSMB detected in the affinity-purified fraction containing ubiquitinated sperm proteins. Based on our results, we conclude that UPS does not appear to be the regulatory mechanism in the case of MSMB and opening new questions for further studies. Thus, the capacitation-induced processing of seminal plasma proteins on the sperm surface may be more complex than previously thought, employing multiple proteolytic systems in a non-redundant manner.

scholarly journals The Conjugated Plasma Proteins of the American Cockroach

1960 ◽  
Vol 43 (5) ◽  
pp. 999-1013 ◽  
Author(s):  
A. N. Siakotos
Keyword(s):  
Neutral Lipid ◽  
Protein Fraction ◽  
Plasma Proteins ◽  
Protein Composition ◽  
Paper Electrophoresis ◽  
American Cockroach ◽  
Sterol Content ◽  
Human Fibrinogen ◽  
Plasma Fractions ◽  
Fraction I

Five protein fractions have been separated by paper electrophoresis from the plasma of the American cockroach. With the utilization of various staining procedures several of the plasma fractions were shown to be conjugated proteins. Two of these (fractions II and IV) are readily identifiable by their phospholipid, carbohydrate, and protein composition. A third conjugated protein, fraction III, is characterized by its high neutral lipid and sterol content. This lipoprotein is also sex-specific. Another fraction (I) contains neutral lipid, sterol, and protein but electrophoretically is more mobile than fraction III. Fraction V, the last and least mobile of the normally occurring proteins, possesses electrophoretic properties similar to human fibrinogen.

New antibody immobilization method via functional liposome layer for specific protein assays

2005 ◽  
Vol 21 (5) ◽  
pp. 833-838 ◽  
Author(s):  
H.Y. Lee ◽  
H.S. Jung ◽  
K. Fujikawa ◽  
J.W. Park ◽  
J.M. Kim ◽  
...  
Keyword(s):  
Specific Protein ◽  
Antibody Immobilization ◽  
Protein Assays ◽  
Immobilization Method
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