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At least 1,153 records · Page 64Linked to original sources
PubMed1976

Electrophoresis of human multiple myeloma and Waldenström's macroglobulinemia sera in sodium dodecyl sulfate polyacrylamide gels.

Sera from normal persons and patients with IgA, IgD, IgG, and IgM monoclonal gammopathies were electrophoresed in polyacrylamide gels containing sodium dodecyl sulfate. The gels were stained with Coomassie blue or were used for immunodiffusion. By this method IgG multiple myeloma and IgM Waldenström's macroglobulinemia sera were readily distinguished by electrophoresis alone, whereas IgA and IgD myeloma sera were distinguished by further immunodiffusion against anti-alpha-chain antibody and anti-delta-chain antibody.

Electrophoresis, Polyacrylamide Gel↗
PubMed1976

The separation of plasma lipoproteins using gel electrofocusing and polyacrylamide gradient gel electrophoresis.

Polyacrylamide gel electrofocusing and gradient electrophoresis have been used to separate the lipoproteins in whole plasma and in fractions prepared by sequential flotation in the ultracentrifuge and by precipitation with dextran sulphate and manganous chloride. After the two-dimensional separation, high density lipoproteins appear as a zone showing noticeable heterogeneity with respect to both isoelectric point and molecular weight. Low density lipoproteins are resolved as a compact spot while very low density lipoproteins are visible as a long horizontal streak across the top of the electrophoresis gel. The implications of the technique for the analysis of lipoprotein patterns in pathological plasmas are discussed.

Electrophoresis, Agar Gel↗
PubMed1978

Discrete separation of HDL2 from HDL3 of human serum by means of polyacrylamide gel.

A relatively short, simple procedure is presented to separate serum high-density lipoproteins discretely into the two main classes, those with densities between 1.063 and 1.125 g/ml (HDL2) and those with densities between 1.125 and 1.210 g/ml (HDL3). A 3.5% polyacrylamide gel in 10 cm glass tubes and the use of Tris/glycine buffer, pH 8.4, will accomplish this separation. The components can be identified in several different ways, examples of which are given. This procedure will give rapid and reliable estimations of both HDL2 and HDL3, and can be used to relate their levels and proportional amounts to incidence or risk of atherosclerosis, coronary-artery disease and possibly cancer.

Adult↗
PubMed1978

Identification of placental alkaline phosphatase in human sera using polyacrylamide gel electrophoresis.

Polyacrylamide gradient gel electrophoresis may be used to separate placental alkaline phosphatase from other types of serum alkaline phosphatase. This method, of which specificity is demonstrated by the thermostability and immunological reaction of the placental form, is sensitive enough to detect an activity of 0.02 mU in a sample, and seems suitable for use in investigating placental isoenzyme in serum.

Adult↗
PubMed1978

Rapid quantitative surface immunofixation of proteins in polyacrylamide gels.

A new method is described which allows rapid identification of sub-microgram amounts of protein in polyacrylamide gels. The technique has been applied to samples of cerebrospinal fluid and serum and is suitable for localisation of both discrete protein bands and diffuse zones. Results from cerebrospinal fluid confirm that IgG is localised in the oligoclonal bands seen in multiple sclerosis. Given antibody excess, there is a linear relationship between the amount of protein applied to the gel and the density of the stained immune complexes on the gel surface.

Blood Proteins↗
PubMed1980

Human globin chain separation by isoelectric focusing in ultrathin polyacrylamide gels.

We describe three basic modifications of our previous method for thalassemia screening by isoelectric focusing of heme-free globin chains: the gel thickness is reduced from 2 mm to 240 microns; the level of the detergent Nonidet P-40 in the gels is decreased from 3% to 0.5%; the polyacrylamide slab is covalently fixed to the supporting glass plate by treatment with silane A-174. By the present method the entire focusing process, starting from gel moulding up to gel destaining and drying, is completed within 4 h, a fraction of the time needed in our previous technique. More than a 100 samples can be analyzed per working day. The present technique also affords increased sensitivity: less than 1 microgram protein/band is detected and less than 200 picomol of hemoglobin are needed for each analysis. Band sharpness and resolution in our ultrathin gels is also considerably increased.

Electrophoresis, Polyacrylamide Gel↗
PubMed1982

Urea polyacrylamide gel electrophoresis of PCMB precipitate as a sensitive test for the detection of the unstable hemoglobin subunit.

A sensitive test for the detection of the abnormal subunit of unstable hemoglobins is described. The unstable hemoglobin subunit was selectively precipitated by paramercuribenzoic acid treatment of the carboxy hemolysate, and the precipitate was studied by urea polyacrylamide gel electrophoresis for globin composition. The test enabled the detection of an electrophoretically silent, alpha-chain unstable variant comprising only 1% of total hemoglobin. Other applications included the demonstration of Hb Köln in a cord blood, and the detection and purification of very slightly unstable hemoglobin variants.

Chemical Precipitation↗
PubMed1984

Comparison of tubular proteinuria, using sodium dodecyl sulphate polyacrylamide gel electrophoresis, in patients during methotrexate or aminoglycoside treatment or with cadmium or Balkan nephropathy.

The pattern of proteinuria found in patients during the administration of methotrexate (MTX) or aminoglycosides (AG) and in cadmium or Balkan nephropathy was investigated using the technique of sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). As renal tubular dysfunction increased, measured by the urinary concentration of 4 low molecular mass (LMr) proteins, SDS-PAGE bands appeared in the following order of molecular mass (Mr): 59, 44, 31, then below 31 000. The presence of bands less than 31 000 was not an early indicator of drug-induced renal damage. Tubular proteinuria could be monitored more easily by the serum and urinary measurement of any one of the LMr proteins: alpha-1-microglobulin (alpha 1m), retinol-binding protein (RBP), beta-2-microglobulin (beta 2m), except alpha-1-acid glycoprotein (AGP), than by SDS-PAGE.

Adult↗
PubMed1987

Preparative fractionation of amyloid proteins on a microgram scale by high-performance liquid chromatography and polyacrylamide gel electrophoresis.

Preparative separation of amyloid proteins on a microgram scale is presented. Amyloid fibrils solubilized in aqueous 50% acetonitrile containing 0.1% trifluoroacetic acid, are fractionated by reverse-phase high-performance liquid chromatography. Fractionation of amyloids obtained from patients with familial Mediterranean fever allowed isolation of a protein identical with a conventionally isolated AA-protein. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis is used for preparative separation of AL-proteins. Two protein extraction procedures from Coomassie Blue stained gels are applied using elution in 0.1% sodium dodecyl sulfate containing buffer and 6 mol/l guanidine-HCl solution. The eluted proteins are concentrated and sodium dodecyl sulfate and dye are removed by acetonitrile precipitation of sample.

Amyloid↗
PubMed1989

Bound amino acids in uremic sera: search for peptidic middle molecules by preparative polyacrylamide gel electrophoresis and high performance liquid chromatography.

The samples of normal and uremic sera were ultrafiltered, separated on SEP-PAK C18 cartridges and subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The serum material extracted from the slab gel was purified from SDS and further fractionated by reverse-phase high performance liquid chromatography (HPLC). The obtained fractions were examined by amino acid analysis and mass spectrometry. An increased number of moderately polar fractions containing bound amino acids was found in sera of uremic patients on hemodialysis. Two most prominent uremic fractions corresponded to N-benzoylglycine (hippuric acid) (fraction I, k' = 9,4) and phenylacetylglutamine (fraction II, k' = 9,7). Increased amounts of bound glutamine, glycine, serine, leucine, asparagine, alanine, valine, phenylalanine were found in other moderately polar uremic fractions. These fractions (k' range from 12.1 to 13.2) contained no free amino acids, nor any other known small uremic serum compounds; they were considered as peptide 'middle molecules' (MM) of a molecular mass smaller than 1700.

Amino Acids↗
PubMed1989

Isolation of creatine kinase BB isoenzyme with high specific activity and adequate purity for radioimmunoassay from human placenta on preparative polyacrylamide gel electrophoresis.

This report describes the procedures for isolation of creatine kinase BB isoenzyme (CK-BB) from human placenta on preparative polyacrylamide gel electrophoresis. 2.5 mg of CK-BB was purified from a 100-g portion of the human placenta, which had a mean specific activity of 957 kU/g and a mean yield of 16%. The placenta CK-BB exhibited single protein bands on several electrophoretic techniques. In addition, both of the placenta and brain CK-BB preparations were individually iodinated and the identical immunological properties of both the CK-BB preparations were confirmed in radioimmunoassay.

Autoradiography↗
PubMed1992

A simple, sensitive technique for classification of apolipoprotein(a) isoforms by sodium dodecyl sulphate-polyacrylamide gel electrophoresis.

Lipoprotein(a) (Lp(a)) is a lipoprotein containing a unique glycoprotein, apolipoprotein(a) (apo(a)), which shows considerable heterogeneity of apparent molecular mass on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). A unifying classification of isoform has been lacking. A simple sensitive procedure for classifying apo(a) isoforms was developed in which the relative mobility of apo(a) on SDS-PAGE was related to that of apolipoprotein (apo) B-100 (Rf vs B). After Western blotting apo(a) bands were visualised by a sensitive double antibody technique employing commercial polyclonal antibodies (sheep antihuman Lp(a) antibody, alkaline phosphatase-linked donkey antisheep antibody). The technique was sensitive (lower limit of detection 0.02 micrograms apo(a)) and had good reproducibility (coefficient of variation 0.9-6.4%). Ten isoform mobilities are described (less than 0.35, 0.40, 0.50, 0.60, 0.70, 0.80, 1.0, 1.10, greater than 1.15). Individuals may have single or double band phenotypes. This classification is compatible with those previously described and the method is suitable for many laboratories, as it employs standard equipment and commercially available materials.

Apolipoproteins A↗
PubMed1996

Detection of heparin-like glycosaminoglycans in normal human plasma by polyacrylamide-gel electrophoresis.

This paper describes a procedure that allows detection of endogenous heparin present in normal human plasma by polyacrylamide-gel electrophoresis (PAGE). Plasma was submitted to proteolysis: an antithrombin III-dependent and heparinase I-sensitive anticoagulant activity was demonstrated in the supernatant of the digest. The supernatant was submitted to sequential fractionation with increasing concentrations of ethanol (25%, 50%, 60% and 65%, by vol.). Fractions were analyzed by PAGE for both glycosaminoglycan (GAG) and protein content. GAGs were detected by gradient PAGE (24-30%). The fraction obtained by 60% ethanol precipitation contained heparinase I-sensitive GAG. We show that GAGs co-precipitate with proteins. The SDS-PAGE of the material resulting from proteolytic digestion and subsequent ethanol fractionation, revealed three major bands. These peptides co-precipitated with plasma GAGs, mainly with the fraction obtained by 60% ethanol. We discuss the possibility that circulating endogenous heparin interacts with such peptides.

Electrophoresis, Cellulose Acetate↗
PubMed1976

The effect of cryogenic storage on human erythrocyte membrane proteins as determined by polyacrylamide-gel electrophoresis.

A study was conducted to determine the effects of freezing on the major membrane proteins of isolated human erythrocyte membranes. Membranes in low or normal ionic strength medium were frozen at slow or fast freezing rates. The membrane protein composition and elution of proteins from the membranes were studied utilizing polyacrylamide-gel electrophoresis in a sodium dodecyl sulfate or an acetic acid-urea-phenol solvent system. Neither a change in the composition of the membrane proteins nor any elution of membrane protein during freezing and thawing was observed. The data indicate that any human erythrocyte membrane damage during freezing and thawing was not related to a change in major membrane protein composition. Human red cell membranes were stable at --80 or --196degreesC in the absence of a cryoprotective agent.

Blood Preservation↗
PubMed1985

Effect of aging on human aortic protein composition. I. One-dimensional polyacrylamide gel electrophoretic analysis of tissue extracts.

Proteins extracted from matching areas of homogenized intimas of 17 human aortas, from two age groups (15-34 and 35-82), were studied after separation by polyacrylamide gel electrophoresis, silver staining, and densitometric scanning. Several definite protein bands including 6 major and 16 minor bands were identified in 17 aortic intima samples grossly and microscopically lesion free. However, such electrophoretic patterns were found to differ in the two age groups studied. For instance, (1) the integrated densities (amounts) of protein bands 1, 6, 13, 16, and 19 which we interpreted as of mural vascular origin were significantly higher in the younger age group, whereas the amounts of bands 2, 7, 9, 11, and 21 suspected to be of plasma origin were found to be significantly higher in the older age group; (2) protein band No. 8 was found to be double in the younger age group vs a single line in the older age group, whereas band No. 12 was the opposite. These changes in protein composition appear to correlate closely with diffuse intimal thickening found histologically in older age group, and will be further studied to relate to those in atherosclerotic lesions.

Adolescent↗
PubMed1985

Effect of aging on human aortic protein composition. II. Two-dimensional polyacrylamide gel electrophoretic analysis.

Arterial intima proteins were extracted by 9 M urea from matching histologically atheroma-free areas of 27 human thoracic aortas of both sexes from younger (15-34) and older (35-82) age groups and studied after separation by high-resolution two-dimensional polyacrylamide gel electrophoresis. Seventeen specific protein groups on each gel were identified according to their relative charges and molecular weights and their distribution in the two age groups compared. Some plasma-derived proteins occurred rarely in young aortas while they were consistently found in those from older cases, i.e., protein group 4 (alpha 1-antichymotrypsin) 1/13 (8%) vs 12/14 (86%), group 7 (haptoglobin beta-chain) 1/13 (8%) vs 13/14 (93%) and groups 6 and 9 (IgG chains) 3/13 (23%) vs 9/14 (64%), respectively. Other plasma-derived proteins such as group 3 (albumin) and 5 (alpha 1-antitrypsin) were identified in all samples of both age groups but their expression in the aortic intima increased with age. Proteins which are typically found intracellularly such as those from groups 11 (actin), 12 (cytoskeleton proteins), and 13 (tropomyosin-like proteins) appeared in samples of intima of both age groups but were less apparent in older specimens. These studies suggest that the changes in aortic intima protein distribution in the absence of atherosclerosis closely correlate with histological changes such as intimal thickening often found with aging, providing new sensitive markers of vascular senescence.

Adolescent↗
PubMed1983

Analysis of normal and neoplastic lymphocyte surface-labeled proteins by two-dimensional polyacrylamide gel electrophoresis.

Normal and neoplastic murine and human lymphocytes were surface-labeled by lactoperoxidase-catalyzed radioiodination, and the cell lysates were subjected to two-dimensional polyacrylamide gel electrophoresis (2D-PAGE) analyses, combining isoelectric focusing in the first dimension and sodium dodecyl sulfate-PAGE (SDS-PAGE) in the second dimension. 2D-PAGE autoradiogram patterns were reproducible and reflected differences in cell types. A string of spots with a Mr of 100K was tentatively identified as a new T-cell marker (Tp100) which was present in all murine and human T cells examined including human T lymphomas. Murine and human B cells displayed markers characteristic to B cells of each species with some similarities between them. Human lymphomas and murine cell lines showed markers which were absent or only weakly visible in normal cells. Thus, 2D-PAGE analysis of lymphocyte surface proteins proved to be a method useful for searching for various markers.

Animals↗
PubMed1983

Protein components of rat lens and their age-related changes observed with two-dimensional polyacrylamide gel electrophoresis.

The protein components of rat lens crystallins were analyzed by two-dimensional urea-sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis. The following age-related changes were observed. (i) In alpha-crystallin, one or two spots at the anodic sides of alpha A2 and alpha B2 spots were observed in the lens cortex after the 8 months. beta-Crystallin, consisting of seven components designated as beta-1 to beta-7 components in the case of 1.5-month-old rats, showed marked changes during ageing. Component beta-3 was not detectable in neonatal lens. Component beta-5' located at the cathodic side of component beta-5 was observed in the lens older than 8 months. Components at the anodic sides of beta-4, beta-6 and beta-7 spots were detected in 8-month and especially 19- and 47-month-old lenses. The amount of gamma-crystallin decreased in dependence on age. (ii) The electrophoretogram of the nucleus of 8-month-old lens showed additional spots in the area with the lower molecular weight than alpha A2. gamma-Crystallin was accumulated in the nucleus. The electrophoretogram of gamma-crystallin of the 8-month-old nucleus was more similar to that of 19-month-old lens cortex than that of neonatal lens or young lens cortex.

Aging↗