scholarly journals Proteinuria after Burn Injury

1981 ◽  
Vol 18 (6) ◽  
pp. 353-360 ◽  
Author(s):  
Peter G Shakespeare ◽  
Edward J Coombes ◽  
Joan Hambleton ◽  
Diane Furness
Keyword(s):  
Total Protein ◽  
Burn Injury ◽  
Serum Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Burn Patients ◽  
Tubular Proteinuria ◽  
Glomerular Lesion ◽  
Protein Excretion ◽  
Urine Pool

Qualitative and quantitative aspects of the excretion of protein after burn injury have been investigated. The excretion of total protein and of albumin have been measured nephelometrically while the excretion of proteins of both serum and non-serum origin have been measured by immunoelectrophoresis using antiserum against serum proteins or against a pool of urine from burned patients. Comparison of the patterns of proteins observed in urine using these two different antisera showed the presence of at least three major proteins that did not originate from the plasma. The excretion of two of these three proteins followed closely the pattern of total protein excretion which reached a maximum at five to seven days after injury. The excretion of albumin was greatest in the first 48 hours after injury. Examination of the original burn patients' urine antigen by sodium dodecyl sulphate polyacrylamide gel electrophoresis showed that this urine pool contained greater amounts of lower molecular weight proteins than were observed in a pool of normal urines. The observations suggest that a biphasic renal pathophysiology is observed after burn injury. Initially, there develops a mild transient glomerular lesion which progresses to a different state which shows at least some of the features of a tubular proteinuria.

scholarly journals On the identity of vitronectin and S-protein: immunological crossreactivity and functional studies

Blood ◽  
1986 ◽  
Vol 68 (3) ◽  
pp. 737-742
Author(s):  
BR Tomasini ◽  
DF Mosher
Keyword(s):  
Monoclonal Antibody ◽  
Serum Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Membrane Attack Complex ◽  
Biochemical Properties ◽  
Complex Data ◽  
Heparin Binding ◽  
S Protein

Vitronectin (serum spreading factor), a major serum cell adhesion molecule, was compared with S-protein, the inhibitor of the C5–9 membrane attack complex. Data from the literature indicate that S- protein and vitronectin are alpha globulins with the same aminoterminal residues, amino acid compositions, and concentrations in normal plasma (150 to 250 micrograms/mL). Both proteins have been reported to interact with the thrombin-antithrombin complex. The cDNA sequences of vitronectin and S-protein were recently determined and found to be almost identical. In the present studies, rabbit-anti-S-protein and a monoclonal antibody to vitronectin both recognized 65,000- and 75,000- molecular weight (mol wt) polypeptides when plasma or serum proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and transferred to nitrocellulose paper. The 65,000 and 75,000-mol wt polypeptides bound more avidly from serum than plasma to monoclonal anti-vitronectin or heparin coupled to agarose. The presence or absence of the polypeptides constituted a major difference between the heparin-binding proteins of serum and plasma. When complement- activated serum and unactivated serum were separated by gel filtration, vitronectin coeluted with C9 in high-mol-wt fractions of activated serum but not unactivated serum. Purified S-protein was recognized by the monoclonal antibody to vitronectin and promoted spreading of human skin fibroblasts. Both vitronectin and S-protein were degraded by thrombin. On the basis of immunological and functional, as well as biochemical, properties, therefore, S-protein and vitronectin are the same.

scholarly journals The Effect of Parenteral Infusion of Amino Acids in Burn Patient

2013 ◽  
Vol 24 (1) ◽  
pp. 12-15
Author(s):  
Kamrun Nahar ◽  
Zeba-un Naher ◽  
Matira Khanam ◽  
Shaheen Akhter ◽  
Tahmina Bashar ◽  
...  
Keyword(s):  
Amino Acid ◽  
Serum Albumin ◽  
Total Protein ◽  
Burn Injury ◽  
Burn Patients ◽  
Serum Total Protein ◽  
Female Ratio ◽  
Group I ◽  
The Mean ◽  
Group Ii

Adequate nutritional support may prevent weight loss  following severe burn injury. However, persistently low  levels of serum albumin, transferring and serum total  protein in burn patients have suggested that a protein  deficiency may continue to exist which is out of proportion  to energy requirements.  This interventional study cross sectional study was done in  the Department of Biochemistry, Bangabandhu Sheikh  Mujib Medical University (BSMMU), Dhaka, Bangladesh  during January 2008 to December 2008. A total of 40 acute  burn injury (within 24 hours of burn) patients of 20-45  years age with 15%-30% burn were selected for this study  as case. The study subjects were divided into two groups:  Group I represent superficial burn & Group II represents  deep burn.  The mean age of 28.35±6.81 years and 30.85±7.32 years in  group I and group II respectively. The number of male in  Group-I was 08 and Group-II was 08 and male female ratio  was 2:3. The mean serum total protein before infusion of  amino acid in Group-I was 55.31±3.58 g/L and in Group-II  was 52.01±2.26 g/L (p<0.001). The mean serum total  protein after infusion of amino acid in Group-I was  68.02±2.04 g/L and in Group-II was 61.86±2.49g/L  (p<0.001). The mean serum albumin before infusion of  amino acid in Group-I was 27.6±2.88 g/L and in Group-II  was 25.57±1.89 g/L (p<0.001). The mean serum albumin  after infusion of amino acid in Group-I was 22.29±3.50 g/L  and in Group-II was 19.83±2.86 g/L (p<0.001). In group-I,  serum total protein was increased by 22.98% after infusion  and in group-II, that was increased by 18.94% (p<0.01).  In group-I, serum albumin was decreased by 19.24% after  infusion and in group-II, that was decreased by 22.45%  (p<0.05). Serum total protein significantly increased after  infusion of amino acid but serum albumin significantly  decreased after infusion of amino acid. DOI: http://dx.doi.org/10.3329/medtoday.v24i1.14107 Medicine TODAY Vol.24(1) 2012 pp.12-15

scholarly journals Purification, characterization and inhibition of human skin collagenase

1978 ◽  
Vol 169 (2) ◽  
pp. 265-276 ◽  
Author(s):  
David E. Woolley ◽  
Robert W. Glanville ◽  
Dennis R. Roberts ◽  
John M. Evanson
Keyword(s):  
Human Skin ◽  
Culture Medium ◽  
Serum Proteins ◽  
Specific Activity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Polyacrylamide Gel ◽  
Collagen Fibrils ◽  
Ph Optimum

1. The neutral collagenase released into the culture medium by explants of human skin tissue was purified by ultrafiltration and column chromatography. The final enzyme preparation had a specific activity against thermally reconstituted collagen fibrils of 32μg of collagen degraded/min per mg of enzyme protein, representing a 266-fold increase over that of the culture medium. Electrophoresis in polyacrylamide disc gels showed it to migrate as a single protein band from which enzyme activity could be eluted. Chromatographic and polyacrylamide-gel-elution experiments provided no evidence for the existence of more than one active collagenase. 2. The molecular weight of the enzyme estimated from gel filtration and sodium dodecyl sulphate/polyacrylamide-gel electrophoresis was approx. 60000. The purified collagenase, having a pH optimum of 7.5–8.5, did not hydrolyse the synthetic collagen peptide 4-phenylazobenzyloxycarbonyl-Pro-Leu-Gly-Pro-d-Arg-OH and had no non-specific proteinase activity when examined against non-collagenous proteins. 3. It attacked undenatured collagen in solution at 25°C, producing the two characteristic products TCA(¾) and TCB(¼). Collagen types I, II and III were all cleaved in a similar manner by the enzyme at 25°C, but under similar conditions basement-membrane collagen appeared not to be susceptible to collagenase attack. At 37°C the enzyme attacked gelatin, producing initially three-quarter and one-quarter fragments of the α-chains, which were degraded further at a lower rate. As judged by the release of soluble hydroxyproline peptides and electron microscopy, the purified enzyme degraded insoluble collagen derived from human skin at 37°C, but at a rate much lower than that for reconstituted collagen fibrils. 4. Inhibition of the skin collagenase was obtained with EDTA, 1,10-phenanthroline, cysteine, dithiothreitol and sodium aurothiomaleate. Cartilage proteoglycans did not inhibit the enzyme. The serum proteins α2-macroglobulin and β1-anti-collagenase both inhibited the enzyme, but α1-anti-trypsin did not. 5. The physicochemical and enzymic properties of the skin enzyme are discussed in relation to those of other human collagenases.

Structural polypeptides of cholera bacteriophage

1981 ◽  
Vol 27 (1) ◽  
pp. 72-75 ◽  
Author(s):  
K. Chaudhuri ◽  
M. Maiti
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Total Protein ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Molecular Weights

The structural polypeptides of the cholera bacteriophage [Formula: see text] have been analysed by sodium dodecyl sulphate – polyacrylamide gel electrophoresis. Eight different polypeptides were identified. The apparent molecular weights of the polypeptides were 143 000, 96 500, 68 000, 53 000, 37 500, 29 500, 21 000, and 13 500, respectively. The percentage of total protein corresponding to each polypeptide was estimated.

scholarly journals Purification of a Zinc Binding Protein from Xylem of Citrus jambhiri

2002 ◽  
Vol 127 (5) ◽  
pp. 718-723 ◽  
Author(s):  
Kathryn C. Taylor ◽  
Danielle R. Ellis ◽  
Luciano V. Paiva
Keyword(s):  
Total Protein ◽  
Proteinase Inhibitors ◽  
Binding Protein ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Sulfhydryl Group ◽  
Size Exclusion ◽  
Binding Studies ◽  
Citrus Jambhiri ◽  
Citrus Rootstock

Zinc in xylem and phloem of the citrus rootstock, rough lemon [Citrus jambhiri (L.)] was associated with a Zn-binding protein, designated citrus vascular Zn-binding protein (CVZBP). The apparent molecular mass of the CVZBP was 19.5 kDa after nondenaturing size exclusion chromatography and 21.8 kDa after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Ion exchange chromatography demonstrated that CVZBP was anionic, requiring 0.43 n NaCl for elution from quaternary aminoethyl Sepharose. Antiserum to the protein cross-reacted more with total protein extracts from leaf midveins than with total protein from the rest of the leaf lamina, further suggesting a vascular location of the Zn-binding protein. Quantitative analysis indicated that ≈2 to 3 mol of Zn were associated with 1 mol of native protein. Binding studies with the partially purified CVZBP demonstrated a capacity to bind several divalent cations: Cd, Ni, Pb, and Zn. Reaction with Ellman's reagent suggested that the protein has significant sulfhydryl group content that may be involved in metal binding. N-terminal sequencing demonstrates identity with papaya latex trypsin inhibitor, sporamin, or other Kunitz soybean proteinase inhibitors.

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 Neutrophils from patients after burn injury express a deficiency of the oxidase components p47-phox and p67-phox

Blood ◽  
1996 ◽  
Vol 88 (11) ◽  
pp. 4321-4329 ◽  
Author(s):  
J Rosenthal ◽  
GW Thurman ◽  
N Cusack ◽  
VM Peterson ◽  
HL Malech ◽  
...  
Keyword(s):  
Respiratory Burst ◽  
Oxidase Activity ◽  
Thermal Injury ◽  
Burn Injury ◽  
Sodium Dodecyl ◽  
Burn Patients ◽  
Biochemical Basis ◽  
Free System ◽  
The Status ◽  
Oxidase Enzyme

Infection is a major cause of morbidity and mortality in patients after thermal injury. This predisposition to infections is related, in part, to abnormal polymorphonuclear leukocyte (PMN) function and a diminished respiratory burst. To evaluate the biochemical basis for the defective respiratory burst after major burns, the status of the oxidase enzyme system and its components was investigated. PMNs were isolated from 24 patients with 12% to 62% burns. Oxidase activity of intact PMNs, measured as superoxide anion (O2-) generation or oxygen consumption, was decreased in burn compared with healthy controls. Subcellular fractions from patient PMNs generated less O2- in the sodium dodecyl sulfate cell-free system, and this was related to a diminished contribution by cytosol but not by plasma membrane. Subsequently, cytosol was separated with CM-Sepharose, yielding two fractions; one contained the p47-phox and p67-phox (47/67 mix) and the other contained the remaining cytosolic components (run through [RT]). Although the contribution to oxidase activity made by RT from patient cytosol was similar to that of control, the activity of p47/67 mix from PMNs of burn patients was deficient. Quantitative assays using an immunoautoradiographic technique showed a consistent, but significant decrease in both p47-phox and p67-phox. The addition of purified or human recombinant p47-phox but not p67-phox corrected the diminished oxidase activity of cytosol from burn patients. Thus, decreased respiratory burst activity found in PMNs from individuals with thermal injury was associated with a specific, quantitative deficiency of p47- phox.

Quantitative analysis of serum proteins separated by capillary electrophoresis

1993 ◽  
Vol 39 (4) ◽  
pp. 689-692 ◽  
Author(s):  
J W Kim ◽  
J H Park ◽  
J W Park ◽  
H J Doh ◽  
G S Heo ◽  
...  
Keyword(s):  
Capillary Electrophoresis ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Agarose Gel ◽  
Agarose Gel Electrophoresis ◽  
Serum Samples ◽  
Polyclonal Gammopathy ◽  
Quantitative Analyses

Abstract The possibility of open tubular capillary electrophoresis for clinical diagnostic use is examined. Capillary electrophoresis was performed in an untreated 50 microns (i.d.) x 100 cm (65 cm to detector) capillary with detection of absorbance at 200 nm. Conditions for the separation of serum proteins without adsorption to the capillary surface were established. Quantitative analyses of serum samples from 38 patients with liver cirrhosis, nephrotic syndrome, or polyclonal gammopathy by capillary electrophoresis were done and the results were compared with those by conventional agarose gel electrophoresis and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. All samples were analyzed in duplicate. We evaluated linearity of response, within-run CV, and the correlation between capillary electrophoresis and agarose gel electrophoresis.

Method for measuring the concentration of urinary proteins according to their molecular size category.

1976 ◽  
Vol 22 (5) ◽  
pp. 667-672 ◽  
Author(s):  
A J Pesce ◽  
A Hsu ◽  
C Kornhauser ◽  
K Sethi ◽  
B S Ooi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Low Molecular Weight ◽  
Tubular Proteinuria ◽  
Equal Concentration ◽  
Glomerular Proteinuria ◽  
Low Molecular Weight Proteins

Abstract We combined the use of a concentrating device (Minicon) and polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate to semi-quantitate the concentration of (a) the collective low-molecular-weight proteins and (b) of albumin excreted in the urine of patients after renal transplantation. Analytical recovery of many serum proteins from samples concentrated 100-fold in the Minicon apparatus was about 70%. It was possible to examine many urine samples by polyacrylamide gel electrophoresis after concentration with this device. The reproducibility (CV) of the technique was on the order of 20% when albumin and low-molecular-weight protein were in about equal concentration. The method was adequate to differntiate glomerular and tubular proteinuria, because in glomerular proteinuria the ratio of albumin to low-molecular-weight proteins is about 20/1, whereas in tubular proteinuria the ratio is about 1/1.

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