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At least 109 records · Page 6Linked to original sources
PubMed1997

Characterization of proteinuria in primary glomerulonephritides. SDS-PAGE patterns: clinical significance and prognostic value of low molecular weight ("tubular") proteins.

In 145 patients with focal segmental glomerulosclerosis (43), membranous glomerulonephritis (72), and membranoproliferative glomerulonephritis (30), 71% with normal renal function (NRF) and 63% with nephrotic syndrome (NS), the proteinuria was evaluated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and classified into four main patterns: physiological (termed 70 kd), pure glomerular (150 kd), mixed with low molecular weight (LMW) proteins as low as 23 kd (23 kd), and mixed with very LMW proteins (20 to 10 kd; termed 10 kd). The relative frequencies were 70 kd, 0.7%; 150 kd, 1.4%; 23 kd, 61%; and 10 kd, 37%. Therefore, only the two patterns characterized by LMW ("tubular") proteins were compared to determine whether they have different clinical and prognostic significance. The serum creatinine (sCr) values (P < 0.0001), the degrees of proteinuria (P = 0.007), and the tubulointerstitial damage (P = 0.015) were significantly different in the two subgroups of patients with 23-kd and 10-kd LMW proteinuria; the difference for tubulointerstitial damage was at the limit of statistical significance after Bonferroni correction. In 82 patients with NRF at entry (sCr, 1.00 +/- 0.22 mg/dL; range, 0.6 to 1.4 mg/dL) and a follow-up of 46 +/- 22 months (range, 12 to 84 months), the predictive value of the 23-kd and 10-kd SDS-PAGE patterns on functional outcome (chronic renal failure [CRF] or clinical remission) was evaluated. A total of 12.5% of 64 patients with mixed 23-kd proteinuria and 50% of 18 patients with mixed 10-kd proteinuria developed CRF. At this time, the difference between the survival curves was highly significant (P = 0.0001), as it also was after correction for NS (P = 0.0002). When the statistical analysis was limited to 69 patients with sCr < or = 1.2 mg/dL, the difference was still highly significant (P = 0.0016), as after correction for NS (P = 0.0064). Clinical remission developed in 30% of 64 patients with 23-kd proteinuria and in 33% of 18 patients with 10-kd proteinuria; this difference was not significant. In a retrospective analysis of 20 patients (13 focal segmental glomerulosclerosis and seven membranous glomerulonephritis; 10 with the 23-kd pattern and 10 with the 10-kd pattern) treated with steroids alone or with steroids and cyclophosphamide, 80% of the patients with the 23-kd pattern and 30% of the patients with the 10-kd pattern were responsive to treatment (P = 0.025). The SDS-PAGE patterns of 54 patients with NRF at entry were again evaluated after 48 +/- 22 months: 11 patients who developed clinical remission had changed from a prevalent (91%) 23-kd pattern to a prevalent physiological (55%) or glomerular (36%) pattern; eight patients who had developed CRF showed an increase from 37% to 100% of the 10-kd pattern. In 35 patients with normal and stable renal function (sCr from 1.08 +/- 0.20 mg/dL to 1.06 +/- 0.19 mg/dL) who had persistent proteinuria (20 patients) or NS (15 patients), the rate of the 10-kd pattern increased from 6% to 46% (72% in persistent NS), suggesting an impairment of tubular protein reabsorptive function even without a concomitant impairment of glomerular filtration rate, a phenomenon that can be hypothetically attributed to tubular toxicity of persistent proteinuria. The characterization of proteinuria by SDS-PAGE in primary progressive glomerulonephritis is a useful clinical tool: it can be used to identify the main pathophysiologic determinants of excretion of LMW proteins and it has a predictive value on CRF outcome in patients with NRF, reducing the unpredictability of clinical evolution. In focal segmental glomerulosclerosis and membranous glomerulonephritis, it seems to be of predictive value on responsiveness to therapy; monitoring the SDS-PAGE patterns over time may give some insights into the relationship between the persistent protein loss and the progression of the disease.

Adolescent↗
PubMed2000

Automated ultra-thin-layer SDS gel electrophoresis of proteins using noncovalent fluorescent labeling.

Ultra-thin-layer SDS gel electrophoresis in conjunction with automated laser-induced fluorescence detection is a novel and powerful method for the analysis of fluorophore-labeled proteins. The technique described in this paper employs instant, noncovalent fluorophore labeling by the addition of a fluorescent staining dye to the sample proteins either during or immediately prior to the sample loading process. Thus, the method does not require time-consuming post- or preseparation staining/labeling. By combining the multilane format of SDS polyacrylamide slab gel electrophoresis and the high separation efficiency of capillary SDS gel electrophoresis, ultra-thin-layer SDS gel electrophoresis features rapid, high-throughput, and high-resolution analysis of proteins in the molecular mass range of 14-116 kDa. The good heat dissipation inherent to the ultrathin format enables the use of agarose and agarose-based composite separation matrixes, which can be easily replaced within the separation platform. Labeling efficiency as a function of the concentration of the staining dye, SDS, and proteins is thoroughly discussed. Detection sensitivity of the method was found to be at the low-femtomole level (1.25 ng/band), determined by analyzing a set of serial dilutions of standard proteins. Practical example of molecular mass determination and characterization of a complex protein mixture are also shown.

Autoanalysis↗
PubMed1997

Conformational analysis of LYS(11-36), a peptide derived from the beta-sheet region of T4 lysozyme, in TFE and SDS.

The solution conformation of a peptide LYS(11-36), which corresponds to the beta-sheet region in T4 lysozyme, has been examined in aqueous solution, TFE, and SDS micelles by CD and 1H NMR spectroscopy. Secondary structure predictions suggest some beta-sheet and turn character in aqueous solution but predict a helical conformation in a more hydrophobic environment. The predictions were supported by the CD and NMR studies which showed the peptide to be relatively unstructured in aqueous solution, although there was some evidence of a beta-turn conformer which was maintained in 200 mM SDS and, to a lesser extent, in 50% TFE. The peptide was significantly helical in the presence of either 50% TFE or 200 mM SDS. TFE and SDS titrations showed that the peptide could form helical, sheet, or extended structure depending on the TFE or SDS concentration. The studies indicate that peptide environment is the determining factor in secondary structure adopted by LYS(11-36).

Amino Acid Sequence↗
PubMed2005

Influence of environmental stresses on stability of O/W emulsions containing cationic droplets stabilized by SDS-fish gelatin membranes.

Oil-in-water (O/W) emulsions containing small oil droplets (d32 approximately 0.22 microm) stabilized by sodium dodecyl sulfate (SDS)-fish gelatin (FG) membranes were produced by an electrostatic deposition technique. A primary emulsion containing anionic SDS-coated droplets (zeta approximately -40 mV) was prepared by homogenizing oil and emulsifier solution using a high-pressure valve homogenizer (20 wt % corn oil, 0.46 wt % SDS, 100 mM acetic acid, pH 3.0). A secondary emulsion containing cationic SDS-FG-coated droplets (zeta approximately +30 mV) was formed by diluting the primary emulsion with an aqueous fish gelatin solution (10 wt % corn oil, 0.23 wt % SDS, 100 mM acetic acid, 2.00 wt % fish gelatin, pH 3.0). The stabilities of primary and secondary emulsions with the same oil concentration to thermal processing, ionic strength, and pH were assessed by measuring particle size distribution, zeta potential, microstructure, destabilized oil, and creaming stability. The droplets in secondary emulsions had good stability to droplet aggregation at holding temperatures from 30 to 90 degrees C for 30 min, [NaCl] < or = 100 mM, and pH values from 3 to 8. This study shows that the ability to generate emulsions containing droplets stabilized by multilayer interfacial membranes comprised of two or more types of emulsifiers, rather than a single interfacial layer comprised of one type of emulsifier, may lead to the development of food products with improved stability to environmental stresses.

Animals↗
PubMed2006

Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling.

Apoptosis signaling through CD95 (Fas/APO-1) involves aggregation and clustering of the receptor followed by its actin-dependent internalization. Internalization is required for efficient formation of the death-inducing signaling complex (DISC) with maximal recruitment of FADD, caspase-8/10 and c-FLIP occurring when the receptor has reached an endosomal compartment. The first detectable event during CD95 signaling is the formation of SDS-stable aggregates likely reflecting intense oligomerization of the receptor. We now demonstrate that these SDS-stable forms of CD95 correspond to very high molecular weight DISC complexes (hiDISC) and are the sites of caspase-8 activation. hiDISCs are found both inside and outside of detergent-resistant membranes. The formation of SDS-stable CD95 aggregates involves palmitoylation of the membrane proximal cysteine 199 in CD95. Cysteine 199 mutants no longer form SDS-stable aggregates, and inhibition of palmitoylation reduces internalization of CD95 and activation of caspase-8. Our data demonstrate that SDS-stable forms of CD95 are the sites of apoptosis initiation and represent an important early step in apoptosis signaling through CD95 before activation of caspases.

Amino Acid Sequence↗
PubMed2003

Oxidant and SDS-stable alkaline protease from Bacillus clausii I-52: production and some properties.

AIMS: An investigation was carried out on an oxidative and SDS-stable alkaline protease secreted by Bacillus clausii of industrial significance. METHODS AND RESULTS: Maximum enzyme activity was produced when the bacterium was grown in the medium containing (g l-1): soyabean meal, 15; wheat flour, 10; liquid maltose, 25; K2HPO4, 4; Na2HPO4, 1; MgSO4.7H2O, 0.1; Na2CO3, 6. The enzyme has an optimum pH of around 11 and optimum temperature of 60 degrees C. The alkaline protease showed extreme stability towards SDS and oxidizing agents, which retained its activity above 75 and 110% on treatment for 72 h with 5% SDS and 10% H2O2, respectively. Inhibition profile exhibited by phenylmethylsulphonyl fluoride suggested that the protease from B. clausii belongs to the family of serine proteases. CONCLUSIONS: Bacillus clausii produced high levels of an extracellular protease having high stability towards SDS and H2O2. SIGNIFICANCE AND IMPACT OF THE STUDY: The alkaline protease from B. clausii I-52 is significant for an industrial perspective because of its ability to function in broad pH and temperature ranges in addition to its tolerance and stability in presence of an anionic surfactant, like SDS and oxidants like peroxides and perborates. The enzymatic properties of the protease also suggest its suitable application as additive in detergent formulations.

Bacillus↗
PubMed2006

Differentiation of proteins based on characteristic patterns of association and denaturation in solutions of SDS.

This paper shows that proteins display an unexpectedly wide range of behaviors in buffers containing moderate (0.1-10 mM) concentrations of SDS (complete unfolding, formation of stable intermediate states, specific association with SDS, and various kinetic phenomena); capillary electrophoresis provides a convenient method of examining these behaviors. Examination of the dynamics of the response of proteins to SDS offers a way to differentiate and characterize proteins. Based on a survey of 18 different proteins, we demonstrate that proteins differ in the concentrations of SDS at which they denature, in the rates of unfolding in SDS, and in the profiles of the denaturation pathways. We also demonstrate that these differences can be exploited in the analysis of mixtures.

Animals↗
PubMed1975

Binding isotherms of sodium dodecyl sulfate to protein polypeptides with special reference to SDS-polyacylamide gel electrophoresis.

To clarify the mode of interaction between sodium dodecyl sulfate (SDS) and protein polypeptides with special reference to SDS-polyacrylamide gel electrophoresis, the binding of SDS to several protein polypeptides was investigated by the equilibrium dialysis technique. Each of the binding isotherms was characterized by the presence of two phases: an initial gradual increase in the amount of binding to 0.3-0.6 g/g (first phase) and a subsequent steep increase to 1.2-1.5 g/g (second phase). The binding was completed at a concentration of SDS below the critical micelle concentration. Throughout the first and second phases, the isotherms obtained were different for each kind of protein. On the basis of experiments with bovine serum albumin and ribonuclease (EC 3.1.4.22], the isotherms were profoundly affected by the method used for modification of the sulfhydryl groups. The claim of Reynolds and Tanford (Proc. Natl, Acad. Sci. U.S., 66, 1002 (1970)) that the isotherms are virtually identical for many kinds of proteins was not supported by the present data. Changes in the gross and local conformations were examined with reference to the isotherms by measurements of CD spectrum, free boundary electrophoresis, and gel filtration. The results obtained were collectively interpreted based on the model of SDS-protein polypeptide complexes proposed by the present authors (J. Biochem., 75, 309 (1974)).

Amylases↗
PubMed1998

Purification of a novel type of SDS-dependent protease in maize using a monoclonal antibody.

A protease which was activated by SDS was purified to homogeneity from maize leaves. On the basis of its proteolytic activity towards ribulose-1,5-bisphosphate carboxylase/ oxygenase (Rubisco) or a synthesized peptide, the purification was carried out using immunoaffinity chromatography with a monoclonal antibody raised against a partially purified enzyme by native gradient PAGE. The purified protease showed three bands at 40, 15, and 13 kDa on SDS-PAGE, indicating that it was composed of heterogeneous subunits. The protease was specifically activated by SDS (optimum = 0.4% for Rubisco proteolysis), but not by poly-L-lysine, fatty acids, or ATP. The protease had a pH optimum around 4.9. beta-Mercaptoethanol stimulated the activity only in the presence of SDS. The proteolytic activity was sensitive to E-64 and leupeptin but was resistant to EDTA, suggesting that the enzyme was an SH-protease. Thus, this enzyme is a novel type of SDS-dependent protease which differs from proteasome, matrix metalloproteinase, and other proteases reported in many organisms.

Animals↗
PubMed1984

Immunological detection of Plasmodium knowlesi antigens after electrophoretic transfer from SDS-polyacrylamide gels to diazophenylthioether paper.

Freeze-thawed extracts of mature schizonts of Plasmodium knowlesi (strain W1) were electrophoresed in sodium dodecylsulphate (SDS) polyacrylamide gels, then transferred electrophoretically to diazophenylthioether paper. The transferred antigen was probed using a purified polyvalent, polyclonal immune serum pool isolated from rhesus monkeys (Macaca mulatta). This method for identifying parasite antigens was compared with immunoabsorption, using parasites which had been metabolically labelled in vitro with 35S-methionine. The methods showed general correspondence but some antigens failed to react after transfer because of loss of antigenicity during SDS-polyacrylamide gel electrophoresis (SDS-PAGE). Some antigens were observed preferentially after the transfer procedure, possibly because of their failure to elute from the immunoabsorbant or because they may have a low methionine content. The transfer method failed to reveal the antigen reactivity of three out of four monoclonal antibodies tested, apparently because the epitopes involved were inactivated by SDS. During P. knowlesi infection in the resistant kra monkey (Macaca fascicularis) the transfer method showed the presence by day 10 of antibodies against two components having an apparent molecular weight by SDS-PAGE similar to those of putative protective antigens described in other studies using monoclonal antibodies.

Animals↗
PubMed1997

Comparative study of chicken and human parathyroid hormone-(1-34)-peptides in solution with SDS.

Molecular conformations of chicken [cPTH-(1-34)] and human [hPTH-(1-34)] parathyroid hormone fragments in aqueous solutions with various concentrations of SDS were investigated by CD, fluorescence and NMR spectroscopy techniques. In the presence of SDS, chicken and human PTH-(1-34) adopt an a-helical structure making up 32-38% of all the peptide amino acids. The process of the a-helical formation of these two fragments is considerably different. The CD spectral change of hPTH-(1-34) was characteristic of a monotonous increase in the negative peak at 222 nm with increasing SDS concentrations. However, for cPTH-(1-34) a beta-turn is formed first, followed by alpha-helix formation upon an increase in SDS concentrations. The change of the tryptophan fluorescence spectra of cPTH-(1-34) is well correlated with the changes in CD spectra, suggesting that the side chain of Trp23 is involved in the conformational change from random coil to alpha-helix via beta-turn. The three-dimensional structure of cPTH-(1-34) with SDS micelle was elucidated by 1H-NMR at pH 3.8 and 300 K, with the combined use of distance geometry and restrained molecular dynamics calculations. NMR results indicated that it contains two helices encompassing residues 7-12 and 24-30, respectively. The C-terminal helix in the residue range of 24-30 is amphiphilic, which is stabilized by the hydrophobic interactions among Trp23, Leu24 and Lys27.

Amino Acid Sequence↗
PubMed2001

Acute toxicity of anionic surfactants sodium dodecyl sulphate (SDS) and linear alkylbenzene sulphonate (LAS) on the fertilizing capability of gilthead (Sparus aurata L.) sperm.

In the present work we have evaluated and compared the acute toxicity of two anionic surfactants, Sodium Dodecyl Sulphate (SDS) and Linear Alkylbenzene Sulphonate (LAS) on the fertilizing capability of gilthead Sparus aurata L. sperm. The criterion used to judge exposure effectiveness was fertilization success. Spawned eggs and sperms were collected from adult giltheads. Sperms were dosed separately with different concentrations of SDS and LAS for 60 minutes. After this period, sperms and eggs were combined for 20 minutes during which fertilization took place. Finally, the number of fertilized eggs were counted and recorded to estimate the percentage of fertilization. Exposure to SDS and LAS concentrations of 0.3, 0.6, 1.5, 3 and 6 mg/L for 60 minutes caused a significant inhibitory effect on fertilization success in gilthead Sparus aurata L.. In addition, the EC50 value for gilthead fertilization after sperm exposure was found to be 2.8 mg/L and in the case of LAS it was of 2.6 mg/L. The comparison of the results from SDS and LAS shows that the latter has a stronger negative effect on sperm viability than SDS.

Alkanesulfonic Acids↗
PubMedDate not supplied

SDS purification of porcine H,K-ATPase from gastric mucosa.

A highly purified membrane fraction of H,K-ATPase was isolated from hog gastric mucosa by using differential centrifugation, sodium dodecyl sulfate (SDS:0.125%) treatment and density-gradient centrifugation. The final fraction showed a major band at 97 kD by SDS-gel electrophoresis. This purified H,K-ATPase sedimented at the interface of a 28-35% sucrose step gradient and displayed a specific activity of 140-170 mumol Pi/h/mg protein and a ratio of K-stimulated ATPase activity to Mg-stimulated ATPase activity of 6.5-8.7. The apparent Km for ATP was 0.154 mM and the Km for K+ was o.6 mM. The enzymatic activity recovered from this purification procedure was K(+)-ionophore-independent. SDS treatment in the presence of 2.5 mM ATP did not change the kinetic properties of the isolated enzyme. Exclusion of ATP during SDS solubilization diminished the enzymatic activity by 90%, indicating that ATP protection is essential for the full recovery of enzymatic activity. In summary, mild SDS solubilization can be used to purify relatively large quantities of active H,K-ATPase to near homogeneity without altering the enzyme's kinetic properties.

Adenosine Triphosphatases↗
PubMed2005

Effects of SDS, PBS solutions upon fluorescence values of Dermatophagoides pterronyssinus radioallergosorbent test inhibition.

OBJECTIVE: To explore the effects of SDS, PBS re-dissolvent solutions on fluorescence values of radioallergosorbent test (RAST) inhibition. METHODS: Dermatophagoides pterronyssinus allergen immunoCAP and UniCAP 100 System were used. The Sera Pool consisted of 20 Dermatophagoides pterronyssinus allergic patients sera, their specific IgE fluorescence values were between 12505 and 24776. RESULTS: Fluorescence value percentages decreased: 62.9%, 54.1%, 43.5%, 6.7%, 3.7%, 2.6%, 2.2%, and 1.4% respectively, when SDS concentrations were at 2%, 1%, 0.5%, 0.25%, 0.1%, 0.05%, 0.025%, and 0.01%. Fluorescence values decreased more than 5% with SDS concentrations equal to 0.25% or higher. PBS in 0.1 and 0.01 mol/L concentrations decreased fluorescence values 2.9% and 0.9% respectively. CONCLUSIONS: SDS is a commonly used surfactants in allergen extract and re-dissolvent prepared allergen precipitation for RAST inhibition. Thus effects of surfactants (e.g. SDS) upon the RAST inhibition tests must be considered when they were used as re-dissolvent agents to improve protein resolution in RAST inhibition.

Allergens↗
PubMed2005

[Electrophoretic analysis (SDS PAGE) of ovulatory cervical mucus in patients with fertility failure and after unsuccessful IVF].

OBJECTIVE: To evaluate the presence and activity of local sperm antibodies and electrophoretic analysis of ovulatory cervical mucus (OCM) to prove the correlation of results of Kremer mucus sperm capillary penetration test and i-MAR (mixed antiimmunoglobulin reaction) test with SDS-PAGE. DESIGN: Retrospective study. SETTING: Department of Obstetrics and Gynecology, Medical Faculty of Charles University, Pilsen. METHODS: 94 patients aged 22-40 (average age 32.3 years) were chosen for our study. Ovulatory cervical mucus was taken from uterine cervical canal in Consultation for Reproductive Immunology. Kremer test and indirect mixed antiglobulin reaction test for IgG, IgA, IgM and IgE were used for detection of sperm antibodies. For the SDS-PAGE analysis, OCM was incubated with sodium dodecyl sulfate. We studied separated protein fractions from OCM. RESULTS: Sperm-capillary ovulatory mucus penetration test (Kremer) was 0-10 cm/hour in our group (average value in patiens without sperm antibodies was 2.43 cm/hour, with sperm agglutinating antibodies 1.4 cm/hour), significant levels (> 45%) of spermagglutinating antibodies were detected in IgA in 6 patients (6.38%), IgG in 5 (5.32%) patients, sperm-cytotoxic levels (IgA and/or IgG) in 5 patients (5.32%); levels of IgE less than 30% in 3 patients (3.19%). Individual immunological factors gained by SDS-PAGE showed the spectrum of various molecular weights with range of 14.4- 350 kDa. The presence of IgG and/or IgA was in 53 cases (56.38%), with 13 ASA positivities (24.53% correlation with i-MAR test) and no ASA activity in 40 cases (75.47%); 6 ASA positive patiens (31.58%) were not detected by SDS-PAGE. CONCLUSIONS: Analysis of 94 OCM by SDS-PAGE showed several significant correlates, but their specifications will be based on further immunoblot research.

Adult↗
PubMed2006

[Study on interaction of anionic surfactant SDS and bovine serum albumin by fourier transform infrared spectroscopy].

FTIR spectroscopy was applied to investigate the interaction of anionic surfactant Sodium Dodecyl Sulfate (SDS) and Bovine Serum Albumin (BSA). Amide band I of BSA was analyzed to obtain the change in secondary structure of BSA when different concentration of SDS was added and during different interaction period. In short interaction period and at low concentration of SDS, the alpha-helixes increased and the random coil decreased. In long interaction period or at high concentration of SDS, SDS unfolded the protein by decreasing the alpha-helix structure and increasing the random coil.

Animals↗
PubMed1990

Comparison of adenoviral hexon polypeptides (monomers) and of native hexons (trimers) by SDS-polyacrylamide gel electrophoresis.

Purified hexons of 27 serotypes of human, simian, bovine and avian adenoviruses were analysed by SDS-PAGE. The apparent molecular weights of hexon polypeptides calculated by comparison with 5 non-hexon and 3 sequenced hexon polypeptide markers ranged from 98 kDa (for bovine adenovirus Ad bos7) to 118 kDa (for simian adenovirus Ad sim13; SV36). A stability of native hexon capsomers (trimers) in SDS at room temperature permitted us to resolve native (trimeric) hexon by SDS-PAGE and to distinguish them from denatured (monomeric) hexon polypeptides by electrophoretic mobilities. Hexon trimer bands with slow mobility in SDS-PAGE (unlike hexon monomer polypeptide bands) retained native hexon antigenicity as revealed by immunoblot analyses. Possible applications of simultaneous analyses of hexon trimers and monomers by SDS-PAGE are discussed.

Adenoviridae↗
PubMed1989

[Differentiation of renal and postrenal hematuria and proteinuria with SDS polyacrylamide gel electrophoresis and immunoblotting].

The pattern of serum proteins separated by SDS-PAGE is typified by the microprotein apolipoprotein A I which is split from high density lipoprotein by SDS. High density lipoprotein is generally retained by the glomerulus and does not appear in the urine even in glomerulopathies. Thus, apolipoprotein A I is generally absent in the SDS-PAGE protein pattern of renal proteinurias. However, in postrenal hematurias and proteinurias apolipoprotein A I can be found by SDS-PAGE, immunoblotting and Ouchterlony test. Using rabbit anti-human-apolipoprotein A I as primary antibody and alkaline phosphatase-conjugated anti-rabbit immunoglobulins as secondary antibody antibody apolipoprotein A I could be detected even at a 1:128,000 dilution of blood. This means a microhematuria of only 8 microliters blood/l urine theoretically can be identified as postrenal. Unfortunately, apolipoprotein A I is not only visible on the immunoblots of postrenal hematurias and proteinurias but could also be seen in renal proteinurias. Thus, only with reservation can apolipoprotein A I be called a marker of postrenal hematuria and proteinuria. On the other hand, most renal proteinurias can be identified reliably by SDS-PAGE and analysis of apolipoprotein A I is superfluous. Apolipoprotein A I, however, could become useful in the differentiation of microhematurias without proteinuria.

Apolipoprotein A-I↗