Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0272170 (SDS)
 50,377 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The acetylcholinesterase was purified by CM-Sephadex chromatography and affinity chromatography on Sepharose bound m-[6-(6-aminocaproylamino)caproylamino]phenyltrimethylammonium bromide. The purified enzyme was obtained with a specific activity of 5470 U/mg (1160-fold purification) and a 89% yield. The molecular weight of the native enzyme was estimated to be 144,000. The enzyme is split into two subunits of approximately equal molecular weight (Mr 69,000) by SDS treatment. It is a glycoprotein and can be resolved by disc gel electrophoresis into seven and by isoelectric focusing into more than ten multiple forms. The N-terminal amino acid is serine.
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PMID:[Purification by affinity chromatography and properties of the acetylcholinesterase of formosan cobra (Naja naja atra) venom (author's transl)]. 53 51

Fibronectin mRNA has been partially purified by guanidine extraction, oligo-(dT)-cellulose chromatography and sucrose density gradient centrifugation. We obtain a fraction which programs a wheat germ in vitro translation system to synthesize a polypeptide species which co-electrophoreses with fibronectin in SDS-polyacrylamide gels and which is immunoprecipitated with affinity purified fibronectin-specific IgG. Analysis of this RNA fraction by methyl mercury hydroxide-agarose gel electrophoresis reveals the presence of a band accounting for 30 percent to 50 percent of the ethidium bromide-staining material in the fraction. The RNA of this band has an estimated molecular weight of about 3 million daltons and is greatly reduced in the corresponding RNA fraction from RSV transformed CEF. This RNA has been tentatively identified as fibronectin mRNA.
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PMID:Partial purification and characterization of the messenger RNA for cell fibronectin. 57 88

The collagen type composition of normal and pathologic scars was examined in comparison with normal skin from the same individual. Particular care was taken to separate scar tissue from adjacent normal dermis. After urea extraction, the tissue specimens were cleaved with cyanogen bromide. The presence of the dermal collagen types I and III was deduced from the electrophoretic distribution patterns of the CNBr peptides in 12% SDS-polyacrylamide gels. The intensity of the type III specific peptide bands correlates with the type III content of the samples. Using this method, the presence of both type I and III collagen can be proved in normal as well as pathologic scars. The type III content in older normal scars is slightly increased, whereas the type III content of pathologic scars is significantly increased in comparison with the type III content of normal skin. The electrophoretic CNBr peptide distribution pattern of pathologic scar tissue is almost the same as that of fetal skin. Both are clearly different from the peptide pattern of normal adult skin.
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PMID:Collagen polymorphism in pathologic human scars. 63 74

Intermediate (8--9 nm) filaments of human central nervous system astrocytes were isolated from the gliosed white matter of cases of adrenoleukodystrophy (ALD). This hereditary lipidosis is characterized pathologically by demyelination, loss of axons, and replacement of the white matter of the caudal cerebrum by a glial scar. Glial filaments were composed largely of a single protein component with a mol wt of about 49,000 daltons. Smaller components (44,000--39,000 daltons) were detected in some samples, and appear to represent degradation products of the filament protein. Human neurofilaments were isolated from the normal frontal white matter of ALD cases by the standard myelin-free axon technique. Isolated glial and neurofilament proteins comigrated during acrylamide gel electrophoresis in SDS. Polypeptides resulting from cyanogen bromide cleavage of the two filament proteins were the same. Both proteins reacted with rabbit antisera raised against isolated bovine neurofilament protein and human glial fibrillary acidic protein.
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PMID:Isolation and characterization of glial filaments from human brain. 69 Jan 74

An acid protease from Monascus kaoliang was purified by consecutive applications of fractional acetone precipitation, batchwise CM-cellulose method and DEAE-cellulose column chromatography. The preparation was homogeneous on disc polyacrylamide gel electrophoresis at pH 4.5 and 7.5. The yield was about 30% with overall increase in specific activity of about 6-fold. The molecular weight as determined by SDS gel electrophoresis was about 34,000. The enzyme was a glycoprotease as indicated by specific carbohydrate staining on gels. It possessed the nature of an acid protease with a pH optimum at 3.0 toward heat-denatured casein and was stable over the range of pH 3.0 to 6.0. Reducing agents and thiol poisons had no effect on this enzyme, suggesting that free sulfhydryl groups were not required for enzyme activity. Diisopropyl fluorophosphate did not inactivate this protease, indicating the probable absence of serine residue in the active site. The enzyme was inactivated by reaction with the carboxy-group specific reagent, 1,2-epoxy-3-(p-nitrophenoxy) propane (EPNP). Pepstatin, a specific inhibitor for pepsin, was shown to inhibit this enzyme strongly. However, biacetyl (2,3-butadione) had little effect on this protease, although it inactivated pepsin to an 85% activity loss. Also, p-bromophenacyl bromide, another specific inhibitor of pepsin, failed to inactivate this acid protease.
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PMID:Purification and characterization of an acid protease from Monascus kaoliang. 74 88

The adsorption of CTAB (cetyltrimethylammonium bromide) to the rat erythrocyte membrane was studied by determining the electrophoretic mobility of erythrocytes treated with CTAB and by SDS polyacrylamide electrophoresis of membrane proteins from erythrocytes treated with 14C-CTAB. At low concentrations of CTAB there was only a small reduction in the electrophoretic mobility of the erythrocytes. At lytic concentrations the electrophoretic mobility of the erythrocytes was markedly reduced. Alterations at the cell surface were found to be a more likely reason for the reduction in the electrophoretic mobility than interactions between the surfactant and charged groups at the cell surface. Very small amounts of radioactivity were found to be associated with the protein and sialoglycoprotein bands of the polyacrylamide gels. It is suggested that the adsorption of CTAB to the rat erythrocyte membrane does not involve electrostatic interactions between the surfactant and negatively charged groups of the sialoglycoproteins and that membrane proteins do not play a major role in the lytic events.
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PMID:The binding of CTAB, a cationic surfactant, to the rat erythrocyte membrane. 76 Mar 86

A new, simple method has been developed for the purification of Streptomyces griseus trypsin [EC 3.4.21.4] from Pronase. Only a single operation of affinity chromatography on an agarose derivative, which was easily prepared by coupling a tryptic digest of salmine to cyanogen bromide-activated Sepharose 4B, was required. A high degree of homogeneity was demonstrated for the purified enzyme by disc electrophoresis, SDS-polyacrylamide gel electrophoresis and gel filtration, as well as by active-site titration. The behavior of a carboxypeptides B [EC 3.4.12.3]-like enzyme present in Pronase is also discussed.
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PMID:Affinity chromatography of trypsin and related enzymes. III. Purification of Streptomyces griseus trypsin using an affinity adsorbent containing a tryptic digest of protamine as a ligand. 81 28

Procollagen and collagen were isolated from the culture medium and cell layer of line TSD4 (obtained from mouse teratocarcinoma OTT6050). SDS-polyacrylamide gel electrophoresis of the highly purified procollagen fraction demonstrated that the fraction is composed of theta chains (150,000 daltons), pro alpha chains (130,000 daltons), and alpha chains (100,000 daltons). Limited pepsin digestion of this fraction yielded a single species of collagen molecules having a chain composition (alpha1)3, as did collagen isolated from the cell layer. Each alpha1 chain appears to be slightly larger than alpha1 chains from calf or human type I and type III collagen. Amino acid analysis and cyanogen bromide peptide profiles of pepsin-treated TSD4 collagen demonstrated significant differences from those of other collagens (II, III, IV) of the type alpha1(X)3, although similar to that of the alpha1 chain of type I collagen, [alpha1(1)]2alpha2. Taken together, acrylamide gel electrophoresis, amino acid composition, electron microscopy, and cyanogen bromide peptide analysis indicate that this material represents a new molecular species of collagen not previously characterized, probably related to [alpha1(I)]3.
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PMID:Procollagen and collagen produced by a teratocarcinoma-derived cell line, TSD4: evidence for a new molecular form of collagen. 83 50

Cytokinin binding protein was isolated and purified from tobacco leaves by bioaffinity chromatography on a Sepharose column on which benzyladenine (BA), synthetic cytokinin, had been introduced as an affinity ligand by the cyanogen bromide method. The purified protein bound specifically to cytokinins; its binding was inhibited remarkably by the addition of BA and kinetin and slightly by adenine, but not by adenosine in vitro. The dissociation constant, Kd, of the protein-BA complex was about 4 x 10(-5)M. The profiles of SDS polyacrylamide gel electrophoresis and gel filtration indicate that the protein consisted of a single polypeptide chain. Amino acid analysis showed that the protein contained 4 basic, 6 acidic, and 25 neutral amino acids but lacked tryptophan. The molecular weight of the protein was determined to be about 4,000 to 5,000 daltons by gel filtration, SDS polyacrylamide gel electrophoresis and amino acid analysis. The coupling conditions of BA to Sepharose by the cyanogen bromide method are described and discussed.
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PMID:Isolation of cytokinin binding protein from tobacco leaves by bioaffinity chromatography and its partial characterization. 86 70

A sodium dodecylsulfate-polyacrylamide electrophoretic method, which in contrast to other biochemical procedures, e.g. differential salt precipitation or ion exchange chromatography and molecular sieve chromatography, is applicable to smallest amounts of protein, is shown to be suitable for the determination of the collagen types from small skin samples, such as routine skin biopsies. After urea extraction, the tissue samples are cleaved with cyanogen bromide. The resulting CNBr peptides derived from the different alpha-chains are resolved in 12% SDS-polyacrylamide gels. Densitometric profiles of the gel electrophoretic patterns correspond to the collagen type content of the tissue specimens. Comparing fetal to adult skin, the higher content of type III collagen in the case of fetal skin can be demonstrated.
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PMID:SDS-polyacrylamide gel electrophoretic determination of type I and type III collagen in small skin samples. 88 41


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