scholarly journals Serum protein concentrations, including acute phase proteins, in calves with hepatogenous photosensitization

2007 ◽  
Vol 59 (6) ◽  
pp. 1355-1358 ◽  
Author(s):  
J.J. Fagliari ◽  
M. Passipieri ◽  
H.T. Okuda ◽  
S.L. Silva ◽  
P.C. Silva
Keyword(s):  
Serum Protein ◽  
Acute Phase ◽  
Serum Proteins ◽  
Acute Phase Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Clinical Signs ◽  
Control Group ◽  
Molecular Weights ◽  
Therapeutic Procedures

One hundred 6- to 12-month-old Nelore calves were allotted into control group (G1; 50 healthy calves) and photosensitization group (G2; n= 50). Blood samples were collected 12 to 24 hours after the onset of dermatitis (M1), and 15 to 30 days after that (M2), at time of resolution of clinical signs. Serum protein electrophoresis was performed by means of sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Eighteen serum proteins with molecular weights ranging from 16,000 to 189,000 daltons (Da) were identified in all calves. In M1 and M2 serum concentrations of proteins with molecular weights of 115,000Da (ceruloplasmin), 61,000Da (a1-antitrypsin), 45,000Da (haptoglobin), and 40,000Da (acid glycoprotein) were significantly increased in calves. In conclusion, measurement of serum acute phase protein concentrations may be useful in monitoring the progression of bovine hepatogenous photosensitization, including guide probable alteration on therapeutic procedures.

scholarly journals Serum protein concentrations, including acute phase proteins, in calves experimentally infected with Salmonella Dublin

2011 ◽  
Vol 31 (7) ◽  
pp. 551-554 ◽  
Author(s):  
Daniela Gomes da Silva ◽  
Péricles Ricardo Lacerda e Silva ◽  
Paulo César da Silva ◽  
José Jurandir Fagliari
Keyword(s):  
Molecular Weight ◽  
Serum Protein ◽  
Serum Proteins ◽  
Acute Phase Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Serum Concentrations ◽  
Salmonella Dublin ◽  
Sds Page ◽  
Holstein Calves

The aim of this study was to evaluate serum protein concentrations in calves experimentally inoculated with Salmonella Dublin. Twelve healthy 10 to 15-day-old Holstein calves were randomly allotted into two groups, control and infected with 10(8) CFU of Salmonella Dublin orally. The calves were subjected to physical evaluation and blood samples were collected shortly before administration of the bacteria and also 24, 48, 72, 96, 120 and 168 hours post-infection. The concentration of serum proteins was determined through sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Thirty serum proteins ranging from molecular weight of 24,000 Da to molecular weight of 236,000 Da were detected. Serum concentrations of ceruloplasmin (125,000 Da), haptoglobin (45,000 Da), acid glycoprotein (40,000 Da) and a 34,000 Da protein were significantly increased in the experimentally infected calves, when compared with their concentrations in the control animals. Therefore, this study showed that S. Dublin infection could lead to the increase of certain serum proteins in calves.

scholarly journals Acute phase proteins in serum and cerebrospinal fluid in healthy cattle: possible use for assessment of neurological diseases

2018 ◽  
Vol 38 (4) ◽  
pp. 779-784 ◽  
Author(s):  
Paula A. Di Filippo ◽  
Saulo T. Lannes ◽  
Marcos A.D. Meireles ◽  
Andressa F.S. Nogueira ◽  
Luiza M.F. Ribeiro ◽  
...  
Keyword(s):  
Cerebrospinal Fluid ◽  
Acute Phase ◽  
Gel Electrophoresis ◽  
Acute Phase Proteins ◽  
Neurological Diseases ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Molecular Weights ◽  
Healthy Cattle

ABSTRACT: Use of acute-phase proteins (APPs) for assessment of health and disease in animals has increased greatly within the last decade. The objective was to determine the normal concentration of APPs in the serum and cerebrospinal fluid (CSF) of healthy cattle by polyacrylamide gel electrophoresis. Fifty crossbred animals (350±70kg of BW and 18±1.2 months of age), 25 heifers and 25 steers were used. CSF samples were collected from atlanto-occipital (AO) site and blood samples were obtained from the jugular vein. CSF and serum protein electrophoresis were performed by means of sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Thirty-seven proteins with molecular weights ranging from 7 and 37kDa were identified in CSF of all animals. These eight were nominally identified with immunoglobulin A and G, celuloplasmin, transferrin, albumin, α1-antitripsin, acidic glycoprotein, and haptoglobin. All protein fractions in CSF did not differ between heifers and steers. In sera, 34 proteins with molecular weights between 7 and 244kDa were identified in heifers and steers. Similar proteins were nominally identified in the sera, but only the CSF presented α1-antitripsin. The serum values of acidic glycoprotein and immunoglobulin G were significantly higher in steers compared with heifers. In conclusion, measurement of CSF acute phase protein concentrations can be useful in diagnosing and monitoring the progression of bovine neurological diseases, perhaps even to guide therapeutic procedures. The CSF electrophoretic profile of healthy cattle does not change depending on gender.

scholarly journals Effects of flunixin meglumine, meloxicam, and firocoxib on the acute-phase proteins in horses following standing castration

2021 ◽  
Vol 41 ◽  
Author(s):  
Paula A. Di Filippo ◽  
Francielli P. Gobbi ◽  
Gabriela B. Lemos ◽  
Célia R. Quirino ◽  
Carla B. Martins ◽  
...  
Keyword(s):  
Acute Phase ◽  
Acute Phase Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Clinical Signs ◽  
Standing Position ◽  
Surgical Trauma ◽  
Markers Of Inflammation ◽  
Flunixin Meglumine ◽  
Anti Inflammatory

ABSTRACT: Excessive infection and inflammation are the most common complications associated with castration. The objective of this study was to compare the efficacy of flunixin meglumine (FM), meloxicam (MX), or firocoxib (FX) for inflammation control after castration in horses using acute-phase proteins (APP) as markers of inflammation. Thirty healthy, unbroken, mixed-breed horses (body weight 358.62±45.57kg and age 4.99±2.63 years) were randomly (n=10 animals/group) allocated to receive one of three different post-castration anti-inflammatory medicines: Group 1 (FM 1.1mg/kg bwt, IV, s.i.d for 5 days); Group 2 (MX 0.6mg/kg bwt, IV, s.i.d for 5 days); and Group 3 (FX 0.1mg/kg bwt, IV, s.i.d for 5 days). All horses were castrated in standing position, using the open technique. Serum and peritoneal APP concentrations were measured by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) and determined before castration (0), and 3, 5, 24, 48, 72, 120 and 168 hours after castration. The results were submitted to analysis of variance using the SAS statistical program, and means were compared by the Student-Newman-Keuls test (p<0.05). Three animals from the MX group developed hyperthermia (with rectal temperatures of 39.8, 39.3 and 38.9°C on day 4, 5 and 6, respectively) and showed local clinical signs of inflammation (inguinal and excessive scrotal edema) and reluctance to walk, as well as a rigid gait of the hind limbs. The same complications were observed in one FX horse. No complications were observed among the FM animals. The castration resulted in significant changes in serum and peritoneal values of total proteins, ceruloplasmin (Cp), transferrin (Tf), albumin (Alb), haptoglobin (Hp) and α1-acid glycoprotein (Gp) in animals of all experimental groups. However, the animals of the MX and FX groups presented more intense acute phase response compared to the animals of the FM group. Changes in the APP were associated with the surgical trauma of castration, but the differences between groups were associated with the ability of the nonsteroidal anti-inflammatory drug to control the inflammation. In conclusion, and based on the findings of acute phase proteins, flunixin is more efficient to control the magnitude of inflammation following castration as compared to meloxicam and firocoxib.

scholarly journals Serum protein concentrations in calves with experimentally induced pneumonic pasteurellosis

2003 ◽  
Vol 55 (4) ◽  
pp. 383-387 ◽  
Author(s):  
J.J. Fagliari ◽  
D.J. Weiss ◽  
D. McClenanhan ◽  
O.A. Evanson
Keyword(s):  
Serum Protein ◽  
Saline Solution ◽  
Acute Phase Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Serum Concentrations ◽  
Pneumonic Pasteurellosis ◽  
Molecular Weights ◽  
Holstein Calves ◽  
Phosphate Buffered Saline

Ten healthy 2 to 4-week-old Holstein calves were randomly allotted into control and infected groups. Control calves (n=5) were inoculated intrabronchially with 5ml of Dulbecco's phosphate-buffered saline solution (DPBSS). Infected calves (n=5) were inoculated intrabronchially with 5x10(9) log-phase Mannheimia haemolytica organisms suspended in 5ml of DPBSS. Blood samples were obtained 15 minutes before and one, two, four and six hours after inoculation. Serum protein concentrations were determined by means of sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Serum concentrations of proteins with molecular weights of 125,000 D (ceruloplasmin), 60,000 D (a 1-antitrypsin), 45,000 D (haptoglobin), and 40,000 D (acid glycoprotein) were significantly increased in calves with pneumonic pasteurellosis, compared with concentrations in control calves. Results indicate that acute phase proteins increase more rapidly after the onset of inflammation than previously thought. Measurement of serum protein concentrations may be useful in monitoring the progression of the induced pneumonic pasteurellosis in calves.

scholarly journals Serum concentrations of acute phase proteins and immunoglobulins of calves with rotavirus diarrhea

2016 ◽  
Vol 68 (4) ◽  
pp. 865-872 ◽  
Author(s):  
T.G. Rocha ◽  
F.D.F. Silva ◽  
C. Bortoletto ◽  
D.G. Silva ◽  
M.G. Buzinaro ◽  
...  
Keyword(s):  
Acute Phase ◽  
Serum Proteins ◽  
Acute Phase Proteins ◽  
Clinical Signs ◽  
Least Square ◽  
Serum Concentrations ◽  
Fecal Samples ◽  
Acid Glycoprotein ◽  
Group B ◽  
Rotavirus Diarrhea

ABSTRACT The aim of the present study was to characterize changes in acute phase protein levels according to the occurrence of rotavirus diarrhea in calves in the first month of life. Blood and fecal samples were taken before colostrum intake and at 1, 2, 7, 15, 21 and 30 days of age from 24 Holstein calves allotted in three experimental groups: calves that did not present diarrhea (group A), calves that presented diarrhea, but tested negative for rotavirus in feces (group B), and calves that presented diarrhea and tested positive for rotavirus in feces (group C) (experiment 1). When the animals presented episodes of diarrhea, blood and fecal samples were taken at 24-hour intervals until the end of clinical signs (experiment 2). Serum proteins were separated by SDS-PAGE technique and rotavirus in feces was detected by PAGE. Data of experiment 1 were analyzed by ANOVA and Tukey's test, considered significant at P<0.05. Data of experiment 2 were subjected to the HSD test. Total protein, globulins, and IgG concentrations were lower in group C than in groups A and B. Ceruloplasmin and transferrin levels were higher in group C than in groups A and B. Serum concentrations of haptoglobin and α1-acid glycoprotein did not differ significantly between groups throughout the experimental period. Calves presented diarrhea between 10.4 and 14.6 days of age in group B, and between 10.3 and 14.6 days of age in group C. In the moments of diarrhea manifestation, least square means of IgA, haptoglobin and α1-acid glycoprotein concentrations did not differ significantly between groups B and C, but ceruloplasmin and transferrin concentrations were higher in group C than in group B, as opposed to what occurred with IgG levels. These findings show that optimizing passive immunity transfer of immunoglobulins decrease the likelihood of calves developing diarrhea caused by rotavirus. In addition, ceruloplasmin presents characteristics of a biomarker of rotavirus infection in calves.

scholarly journals Serum proteins and lipids in mild form of calf bronchopneumonia: candidates for reliable biomarkers

2017 ◽  
Vol 67 (2) ◽  
pp. 201-221 ◽  
Author(s):  
Marijana Kovačić ◽  
Dragana Marković ◽  
Irina Maslovarić ◽  
Sonja Obrenović ◽  
Jelica Grujić-Milanović ◽  
...  
Keyword(s):  
Acute Phase ◽  
Peripheral Blood ◽  
Pasteurella Multocida ◽  
Serum Proteins ◽  
Acute Phase Proteins ◽  
Clinical Signs ◽  
Hdl Cholesterol ◽  
Matrix Metalloproteases ◽  
Γ Globulins ◽  
Biochemical Analyses

Abstract Calf bronchopneumonia is complex multifactorial disease and for its accurate diagnosis and therapy, besides clinical examination, microbiologic, hematologic and biochemical analyses could be necessary. In general, additional analyses are not implemented, mainly because the disease biomarkers are not defined. To establish which analysis might be useful for determining the severity of the disease, we analyzed 23 three-month old calves with mild clinical signs of bronchopneumonia and 15 age-matched healthy calves. Pasteurella multocida was isolated from deep nasal swabs of diseased calves. Peripheral blood erythrocyte and leukocyte count of bronchopneumonic and healthy calves showed no difference. Serum proteins, lipoproteins and lipids were analyzed with spectrophotometry, agarose gel electrophoresis, non-reducing SDS-PAGE, gel zymography, and thin-layer chromatography. The bronchopneumonic calves had an increased level of circulating immune complexes and α globulins, which contain some of the positive acute phase proteins. In diseased calves the increased concentration of total γ globulins (IgG), due to an increased concentration of anionic γ globulins (predominately IgG1), was detected. The increased concentration of anionic γ globulins followed by increased concentration of transferrin (negative acute phase protein) and HDL cholesterol, decreased concentration of LDL-cholesterol, unchanged activity of matrix metalloproteases and leukocyte counts might reflect the obvious absence of generalized inflammation. A positive correlation was found between the acquired results and the appearance of mild clinical signs. Therefore, we believe that the parameters analyzed in the peripheral blood could be applied as reliable disease markers to distinguish between severe (inflammatory) and mild forms of calf bronchopneumonia and to predict a better outcome for these calves.

scholarly journals Allergens from Fusarium solani Identified by Immunoblotting in Asthma Patients In Iran

2012 ◽  
Vol 63 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Ali Khosravi ◽  
Mahnaz Fatahinia ◽  
Hojjatollah Shokri ◽  
Mohammad Yadegari
Keyword(s):  
Fusarium Solani ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Control Group ◽  
Molecular Weights ◽  
Asthmatic Patients ◽  
Sds Page ◽  
Asthma Patients ◽  
Immunoblotting Assay ◽  
Glucose Agar

Allergens from Fusarium solani Identified by Immunoblotting in Asthma Patients In IranWe extracted Fusarium solani antigens to evaluate specific anti-F. solani IgE in fifty-one patients with asthma (33 men and 18 women) and in 22 non-atopic healthy subjects (15 men and 7 women). F. solani strains were cultured in Sabouraud glucose agar and subjected to cell disruption using the freeze-and-thaw method. The obtained cytoplasmic extracts were analysed using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). Sensitisation to F. solani antigens has been evaluated in asthmatic patients using the immunoblotting assay. The SDS-PAGE identified 29 protein bands in the cytoplasmic extracts of F. solani isolates, with molecular weights ranging from 24 kDa to 112 kDa. Immunoblotting detected specific anti-F. solani IgE antibody in all asthma patients, but not in the control group. The predominant reactive allergens in patients corresponded to the bands with molecular weights of 24 kDa, 58.5 kDa, 64.5 kDa, 69 kDa, 72 kDa, and 97 kDa. Our results suggest that various allergenic components of F. solani may produce symptoms of asthma in susceptible individuals and they call for further research.

Low Molecular Weight Trypsin-Plasmin Inhibitors Isolated from Papain Treated Urinary Trypsin Inhibitor

1982 ◽  
Vol 47 (01) ◽  
pp. 014-018 ◽  
Author(s):  
H Sumi ◽  
N Toki ◽  
S Takasugi ◽  
S Maehara ◽  
M Maruyama ◽  
...  
Keyword(s):  
Trypsin Inhibitor ◽  
Gel Electrophoresis ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Chromatography ◽  
Urinary Trypsin Inhibitor ◽  
Plasmin Activity ◽  
Molecular Weights ◽  
Plasmin Inhibitors

SummaryPapain treatment of human urinary trypsin inhibitor (UTI67; mol. wt. 43,000 by SDS-polyacrylamide gel electrophoresis, specific activity 1,897 U/mg protein) produced four new protease inhibitors, which were highly purified by gel chromatography on Sephadex G-100 and isoelectric focusing. The purified inhibitors (UTI26, UTI9-I, UTI9-II, and UTI9-III) were shown to be homogeneous by polyacrylamide disc gel electrophoresis, and had apparent molecular weights of 26,000, 9,000, 9,000, and 9,800, respectively, by sodium dodecyl sulfate gel electrophoresis. During enzymatic degradation of UTI67, the amino acid compositions changed to more basic, and the isoelectric point increased from pH 2.0 (UTI67) to pHs 4.4, 5.2, 6.6, and 8.3 (UTI26, UTI9-I, UTI9-II, and UTI9-III), respectively. Both the parent and degraded inhibitors had anti-plasmin activity as well as antitrypsin and anti-chymotrypsin activities. Much higher anti-plasmin/anti-trypsin and anti-plasmin/anti-chymotrypsin activities were observed in the degraded inhibitors than in the parent UTI67. They competitively inhibited human plasmin with Ki values of 1.13 X 10-7 - 2.12 X 10-6 M (H-D-Val-Leu-Lys-pNA substrate). The reactions were very fast and the active site of the inhibitors to plasmin was thought to be different from that to trypsin or chymotrypsin.

scholarly journals The Archaeal Small Heat Shock Protein Hsp17.6 Protects Proteins from Oxidative Inactivation

2021 ◽  
Vol 22 (5) ◽  
pp. 2591
Author(s):  
Pengfei Ma ◽  
Jie Li ◽  
Lei Qi ◽  
Xiuzhu Dong
Keyword(s):  
Heat Shock ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Small Heat Shock Protein ◽  
Phase Cell ◽  
Molecular Weights ◽  
Oxidative Inactivation ◽  
Methionine Residues ◽  
Shock Proteins ◽  
And Function

Small heat shock proteins (sHsps) are widely distributed among various types of organisms and function in preventing the irreversible aggregation of thermal denaturing proteins. Here, we report that Hsp17.6 from Methanolobus psychrophilus exhibited protection of proteins from oxidation inactivation. The overexpression of Hsp17.6 in Escherichia coli markedly increased the stationary phase cell density and survivability in HClO and H2O2. Treatments with 0.2 mM HClO or 10 mM H2O2 reduced malate dehydrogenase (MDH) activity to 57% and 77%, whereas the addition of Hsp17.6 recovered the activity to 70–90% and 86–100%, respectively. A similar effect for superoxide dismutase oxidation was determined for Hsp17.6. Non-reducing sodium dodecyl sulfate polyacrylamide gel electrophoresis assays determined that the Hsp17.6 addition decreased H2O2-caused disulfide-linking protein contents and HClO-induced degradation of MDH; meanwhile, Hsp17.6 protein appeared to be oxidized with increased molecular weights. Mass spectrometry identified oxygen atoms introduced into the larger Hsp17.6 molecules, mainly at the aspartate and methionine residues. Substitution of some aspartate residues reduced Hsp17.6 in alleviating H2O2- and HClO-caused MDH inactivation and in enhancing the E. coli survivability in H2O2 and HClO, suggesting that the archaeal Hsp17.6 oxidation protection might depend on an “oxidant sink” effect, i.e., to consume the oxidants in environments via aspartate oxidation

Effect of detergents and chemicals on purified vaccinia virus: analysis by SDS polyacrylamide gel electrophoresis and electron microscopy

1977 ◽  
Vol 23 (3) ◽  
pp. 240-252 ◽  
Author(s):  
J. Boisvert ◽  
T. Yamamoto
Keyword(s):  
Electron Microscopy ◽  
Vaccinia Virus ◽  
Gel Electrophoresis ◽  
Alkali Treatment ◽  
Guanidine Hydrochloride ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Ammonium Bromide ◽  
Molecular Weights ◽  
Viral Particles

Vaccinia virus particles were dissociated into their constituent polypeptides and analysed by sodium dodecyl sulfate (SDS) gel electrophoresis. Thirty-three distinct polypeptide bands were identified and their molecular weights ranged between 11 000 and 150 000 daltons.Specific staining of gels containing polypeptides of dissociated virions revealed the presence of eight glycopeptides. No lipopeptides were detected.Analysis of chemical extracts (urea, guanidine hydrochloride, and alkali treatment) of the virus by SDS gel electrophoresis indicated that a total of 10 to 14 different polypeptides ranging in molecular weights from 11 000 to 70 000 daltons were solubilized.Analysis of detergent extracts and of the remains of extracted viral particles has shown that the detergent Nonidet P-40 (NP-40) solubilized a total of 11 polypeptides of which 6 were glycopeptides. The other detergents sodium deoxycholate (SDC) and cetyl trimethyl ammonium bromide (CTAB) were not as selective, both solubilizing more than 25 of the polypeptides composing the virus. Gel electrophoresis results also indicated that most of the small molecular weight (11 000–70 000 daltons) polypeptides were readily solubilized by NP-40, SDC, and CTAB, while those with molecular weights of 70 000 daltons and higher were not well solubilized.The effects of detergents were also analysed by electron microscopy. Evidence was obtained for subpopulations of viral particles having different susceptibility to detergent extraction.

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