scholarly journals Detection of serum proteins in the electrophoretic patterns of total proteins of mycoplasma cells

1976 ◽  
Vol 77 (2) ◽  
pp. 189-198 ◽  
Author(s):  
O. E. Yaguzhinskaya
Keyword(s):  
Culture Medium ◽  
Serum Proteins ◽  
Electrophoretic Pattern ◽  
Sucrose Density Gradient ◽  
Total Proteins ◽  
Molecular Weights ◽  
Electrophoretic Patterns ◽  
Mycoplasma Cell ◽  
Co Precipitation ◽  
Serum Precipitate

SummaryThe contamination of mycoplasma cell preparations by serum proteins originating from culture medium was studied.A. laidlawiiandM. arthritidiscells were grown in the presence of [14C]-aminoacids, and the cells were washed with 0·9% NaCl by threefold centrifugation. Total proteins of the washed cells were analysed by SDS gel electrophoresis. Coomassie-stained electrophoretic patterns were compared with autoradiographs of the same gels. The stained electrophoretic pattern of washedA. laidlawiigrown without serum was identical with autoradiographs of the same cells grown without or with serum. That of washedA. laidlawiigrown with serum differed from the corresponding autoradiograph by the presence of extra protein bands I, II, III, and IV with molecular weights of over 160,000, 80,000–87,000, 55,000 and 25,000, respectively. The same extra bands were found in stained electrophoretic patterns of washed: (a)A. laidlawiicells grown without serum and mixed with serum in the stationary phase, (b)M. arthritidiscells, as compared with their autoradiographs, (c) serum precipitate. The bands III and IV may be due to the heavy and light chains of γ-globulin, the band II might belong to transferrin or to some component of complement. Acidification of serum to pH 5 brought about 100-fold rise of amount of serum precipitate, the number of bands in the electrophoretic pattern of the precipitate being also increased. Stained electrophoretic patterns of cells purified by twofold centrifugation in step sucrose density gradient (1·20–1·27 g./cm.3forA. laidlawii,and 1·15–1·25 forM. arthritidis) contained no extra bands and matched completely with their autoradiographs.It was concluded that contamination of washed mycoplasma cells by serum proteins is mainly due to co-precipitation of aggregated serum proteins together with cells during centrifugation rather than to adsorption of serum proteins on the cell surface.

scholarly journals Serum protein electrophoretic pattern in piglets during the early postnatal period

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Csilla Tóthová ◽  
Robert Link ◽  
Petronela Kyzeková ◽  
Oskar Nagy
Keyword(s):  
Serum Protein ◽  
Serum Proteins ◽  
Protein Pattern ◽  
Electrophoretic Pattern ◽  
Postnatal Period ◽  
Early Postnatal Period ◽  
Total Proteins ◽  
Newborn Piglets ◽  
Γ Globulins ◽  
Protein Electrophoretic Pattern

AbstractThe pattern of serum proteins, the typical features of the electrophoretogram in newborn piglets and during their postnatal development is not completely described. Therefore, the aim of this study was to characterize the changes in serum protein electrophoretic pattern and features of the electrophoretograms during the early postnatal period. Significant changes during the monitored period were found in all evaluated parameters (P < 0.001). The most marked changes were observed mainly in the period before weaning. The concentrations of total proteins, albumin and γ-globulins were before colostrum intake low, γ-globulins represented the smallest proportion of protein fractions. The proportion of α1-globulins was after birth a dominant protein fraction. Significant increase of total proteins, α2-, β- and γ-globulins and decrease of α1-globulins was found 2 days after colostrum intake. The albumin and A/G values increased after birth gradually until weaning. After weaning a significant changes were found in absolute concentrations of total protein and albumin, and in relative values of β-globulin fractions. Presented results showed marked developmental alterations in the serum protein pattern in piglets along with the age. The study also brings new knowledge in the field of description of typical features of electrophoretograms in the observed period of piglet’s life.

Changes in proteins of Domiati cheese during pickling

1972 ◽  
Vol 39 (2) ◽  
pp. 219-225 ◽  
Author(s):  
M. H. Abd El-Salam ◽  
Safinaz El-Shibiny
Keyword(s):  
Amino Acids ◽  
Room Temperature ◽  
Gel Filtration ◽  
Electrophoretic Pattern ◽  
Pasteurized Milk ◽  
Molecular Weights ◽  
Electrophoretic Patterns ◽  
Related Substances ◽  
Nitrogenous Substances

SummaryDomiati cheese from homogenized and unhomogenized pasteurized milk was pickled for 4 months at room temperature. During pickling, the soluble tyrosine and tryptophan contents of the cheese gradually increased, indicating progressive proteolysis.Gel filtration of cheese extract on Sephadex G-25 revealed the presence of nitrogenous substances of various molecular weights. The maximum formation of amino acids and related substances was observed after 15 days storage.The changes in the electrophoretic patterns of proteins in the cheese during pickling indicated that both αs - and β-caseins were attacked. β-Casein, however, was much less affected.Homogenization was found to affect the formation of soluble nitrogenous substances, but was without effect on the electrophoretic pattern of the protein in the cheese.

scholarly journals The electrophoretic pattern of serum proteins in dogs with babesiosis

2019 ◽  
Vol 88 (4) ◽  
pp. 425-432 ◽  
Author(s):  
Csilla Tóthová ◽  
Branislav Lukáč ◽  
Marián Kadaši ◽  
Darina Baranová ◽  
Tatiana Weissová ◽  
...  
Keyword(s):  
Serum Proteins ◽  
Clinical Signs ◽  
Electrophoretic Pattern ◽  
Control Group ◽  
Babesia Canis ◽  
Total Proteins ◽  
Blood Samples ◽  
Γ Globulins ◽  
Healthy Dogs ◽  
G Ratio

This study was aimed at the evaluation of the electrophoretic pattern of serum proteins in dogs naturally infected with Babesia canis. Blood samples were collected from 37 dogs infected with B. canis and showing clinical signs consistent with the disease. The sick animals were classified as dogs with physiologic and decreased red blood cell (RBC) values. Twenty-five healthy dogs formed the control group. The concentrations of total proteins and protein fractions were measured in blood serum. The values of total proteins, albumin and albumin/globulin (A/G) ratio in dogs with babesiosis were significantly lower than in healthy ones (P < 0.001). In the globulin fractions, significantly higher relative concentrations of α1-, β1- and β2-globulins (P < 0.01), and non-significantly higher values of α2- and γ-globulins were found in dogs with babesiosis with a double α2-zone in six out of 37 animals. Marked differences were observed also between the two groups of sick animals, with significantly lower values of albumin and A/G ratio (P < 0.05), and significantly higher values of α1- and β1-globulins in dogs with decreased RBC (P < 0.05 and P < 0.01, respectively). Presented results indicate marked alterations in the electrophoretic pattern of serum proteins in dogs with babesiosis suggesting its usefulness for the evaluation of pathophysiological changes caused by the disease and for diagnostic of disease severity.

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.

The Combining Ability of Glycoproteins IIb, IIIa and Ca2+ in EDTA-Treated Nonaggregable Platelets

1983 ◽  
Vol 50 (04) ◽  
pp. 848-851 ◽  
Author(s):  
Marjorie B Zucker ◽  
David Varon ◽  
Nicholas C Masiello ◽  
Simon Karpatkin
Keyword(s):  
Density Gradient ◽  
Combining Ability ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Electrophoretic Pattern ◽  
Sucrose Density Gradient ◽  
Irreversible Loss ◽  
Sucrose Density Gradient Centrifugation ◽  
Crossed Immunoelectrophoresis ◽  
Triton X

SummaryPlatelets deprived of calcium and incubated at 37° C for 10 min lose their ability to bind fibrinogen or aggregate with ADP when adequate concentrations of calcium are restored. Since the calcium complex of glycoproteins (GP) IIb and IIIa is the presumed receptor for fibrinogen, it seemed appropriate to examine the behavior of these glycoproteins in incubated non-aggregable platelets. No differences were noted in the electrophoretic pattern of nonaggregable EDTA-treated and aggregable control CaEDTA-treated platelets when SDS gels of Triton X- 114 fractions were stained with silver. GP IIb and IIIa were extracted from either nonaggregable EDTA-treated platelets or aggregable control platelets with calcium-Tris-Triton buffer and subjected to sucrose density gradient centrifugation or crossed immunoelectrophoresis. With both types of platelets, these glycoproteins formed a complex in the presence of calcium. If the glycoproteins were extracted with EDTA-Tris-Triton buffer, or if Triton-solubilized platelet membranes were incubated with EGTA at 37° C for 30 min, GP IIb and IIIa were unable to form a complex in the presence of calcium. We conclude that inability of extracted GP IIb and IIIa to combine in the presence of calcium is not responsible for the irreversible loss of aggregability that occurs when whole platelets are incubated with EDTA at 37° C.

Characterization and Partial Purification of Heterodisperse Polysomal RNAs in Normal and Neoplastic Cells

1972 ◽  
Vol 58 (2) ◽  
pp. 71-94
Author(s):  
Ada Sacchi ◽  
Gianni Chinali ◽  
Susetta Pons ◽  
Michela Galdieri ◽  
Piero Cammarano
Keyword(s):  
Size Distribution ◽  
Density Gradient ◽  
Rat Liver ◽  
Sucrose Density Gradient ◽  
Partial Purification ◽  
Messenger Rnas ◽  
Alkaline Ph ◽  
Sedimentation Profile ◽  
Molecular Weights ◽  
Phenol Extraction

The size distribution of cytoplasmic messenger RNAs (m-RNA) has been studied in rat liver and in monodifferentiated cells (mouse reticulocytes and myelomas). It has been found that the RNA which exhibits a « rapid turnover » and a polydisperse profile of radioactivity is refractory to phenol extraction. This property has been exploited to selectively isolate m–RNA from the phenol residue by means of an extraction at an alkaline pH. The sucrose density gradient profiles of m–RNA isolated from monodifferentiated cells show monodisperse peaks having the sedimentation coefficients expected on the basis of the molecular weights of monocistronic messages for α and β chains of hemoglobin (reticulocytes) and L and H chains of immunoglobulin (myelomas). The sedimentation profile of cytoplasmic m–RNA associated with rat liver polysomes shows a much broader distribution, with sedimentation coefficients ranging from 8 S to 28 S.

CHILDHOOD TUBERCULOSIS: CLINICAL VALUE OF THE ELECTROPHORETIC PATTERN OF THE SERUM PROTEINS

PEDIATRICS ◽  
1961 ◽  
Vol 27 (1) ◽  
pp. 54-67
Author(s):  
Rosa Lee Nemir ◽  
Charlotte Marker Zitrin ◽  
Paraskevi Tsouros ◽  
Enriqueta Melly
Keyword(s):  
Serum Protein ◽  
Tuberculous Meningitis ◽  
Gamma Globulin ◽  
Serum Proteins ◽  
Electrophoretic Pattern ◽  
Miliary Tuberculosis ◽  
Protein Fractions ◽  
Reciprocal Relation ◽  
Tuberculous Infection ◽  
Tuberculous Disease

The blood serum protein fractions of 138 children with tuberculosis were analyzed by paper electrophoresis serially over a period of many months. Many manifestations of tuberculous infection were studied. The group was divided into 11 categories ranging from healed or arrested tuberculous disease to various stages of activity. The serum protein fractions were evaluated in terms of prognosis, type of tuberculous disease, effect of intercurrent infection and age of patient. It was found that the greatest changes occurred in the gamma-globulin and albumin fractions in reciprocal relation. With the exception of tuberculous meningitis, the increase in gamma-globulin usually corresponded to the severity of disease. Albumin was correspondingly decreased, and was low even in tuberculous meningitis. Both fractions approached normal levels as the patients improved. Relatively normal readings were found in patients with tuberculosis observation or arrested tuberculosis. The greatest deviation from normal was seen in patients with miliary tuberculosis and those with pleurisy with effusion. Here, the gamma and alpha2-globulins were very high and the serum albumin was low. The alpha2 fraction was elevated in the children with more severe disease, including tuberculous meningitis; with clinical improvement it returned to normal more rapidly than the gamma. A rise in the beta-globulin fraction suggests caseation. Confirmatory evidence was obtained in patients with endobronchial disease, tuberculous adenitis and from the only necropsy in the series. The significant changes in the various fractions are further described and discussed.

scholarly journals Electrophoretic pattern of serum proteins in horses with babesiosis

2010 ◽  
Vol 42 (3) ◽  
Author(s):  
R Barrera ◽  
MV Carapeto ◽  
MA Habela ◽  
C Zaragoza
Keyword(s):  
Serum Proteins ◽  
Electrophoretic Pattern

scholarly journals Differentiation of Colletotrichum gloeosporioides isolates by using total proteins and esterase electrophoretic patterns and extracellular enzymes production

2010 ◽  
Vol 36 (2) ◽  
pp. 140-144 ◽  
Author(s):  
Tereza Cristina de Assis ◽  
Maria Menezes ◽  
Domingos Eduardo Guimarães Tavares de Andrade ◽  
Rildo Sartori Barbosa Coelho
Keyword(s):  
Extracellular Enzymes ◽  
Colletotrichum Gloeosporioides ◽  
Electrophoretic Analysis ◽  
Solid Substrate ◽  
Causal Agent ◽  
Total Proteins ◽  
Anthracnose Disease ◽  
Electrophoretic Patterns

Isolates of Colletotrichum gloeosporioides (ISO-1, ISO-2, ISO-3, ISO-4, ISO-5 and ISO-6), the causal agent of anthracnose disease on mango fruits, were characterized by electrophoretic patterns of total proteins and esterase in polyacrylamida gel, and also, by production of extracellular enzymes on specific solid substrate. The electrophoretic analysis showed variation in number, intensity of coloration and position of the bands in the gel at each studied system tested. In contrast to the monomorphic behavior to total proteins, high esterase polymorfism was observed indicating difference among isolates. All isolates showed the activity of extracellular enzymes such as amylase, lipase, and protease with some variation among them. The proteolitic activity seemed to be more accentuated than the two other enzymes studied.

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