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)

Proline carrier, a product of the putP gene of Escherichia coli, was identified as a 35 kDa cytoplasmic membrane protein by SDS-polyacrylamide gel electrophoresis (SDS-PAGE). Its identification was based on the following evidence: First, the density of the band corresponding to a 35 kDa protein correlated with the proline-binding activity of cytoplasmic membranes from putP-deficient and putP-amplified strains. Second, by the differential labeling method, the 35 kDa protein was specifically labeled with radioactive N-ethyl-maleimide. The 35 kDa protein was found to aggregate on heat treatment and to show abnormal mobility on SDS-PAGE.
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PMID:Identification of proline carrier in Escherichia coli K-12. 390 3

Peptides containing the C-terminus of the alpha-chain of the nicotinic acetylcholine receptor (nAChR), as deduced from cDNA data, were synthesised and shown to bind to antibodies to denatured nAChR. Conversely, peptide-specific antibodies bound both to native and to denatured nAChR. Binding was exclusively to the alpha-chain. Trypsinization experiments and the use of the unique C-terminal hexapeptide of the alpha-chain demonstrated that the proposed C-terminus does exist on the mature alpha-chain, and that post-translational cleavage can be discounted as an explanation of the discrepancy of the molecular masses of the alpha-chain deduced from SDS gel electrophoresis (40 kDa) and from the DNA sequencing (50 kDa). Cleavage of the alpha-chain in the membrane occurs at two closely linked sites, resulting in the formation of a large fragment (approximately 35 kDa) and the remainder of the chain (approximately 9-10 kDa). No signs of experimental myasthenia gravis were observed in rabbits immunised with C-terminal peptide coupled to carrier protein.
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PMID:Antibodies to synthetic peptides as probes of acetylcholine receptor structure. 646 98

Cloned hybrid cell lines secreting antibodies directed against human plasma fibronectin were prepared according to the methods of Kohler and Milstein (Kohler, G. and Milstein, C. (1975) Nature (London) 256, 495-497 and (1976) Eur. J. Immunol. 6, 511-519). The specificity of each monoclonal antibody for fibronectin was established from autoradiograms of radioimmunoprecipitates following SDS-polyacrylamide gel electrophoresis. The monoclonal antibodies were reactive with both native and SDS-denatured fibronectin. Ascites fluids obtained from infected isogenic mice precipitated 85-95% of the 125I-labelled fibronectin radioactivity in indirect radioimmunoprecipitation tests. Localization of specific epitopes to restricted regions of the fibronectin molecule was carried out by monitoring monoclonal antibody binding to proteolytic fragments. Of the five monoclonal antibodies analyzed in this study, three recognized determinants which resided in the terminal 35 kDa region of the fibronectin monomer. Furthermore, these epitopes were localized to fragments as small as 20 kDa. Competition studies carried out using plasma fibronectins isolated from different species revealed that three monoclonal antibodies recognized sites which were relatively conserved, while two monoclonal antibodies recognized epitopic sequences which were unique to the human protein. The corresponding anti-fibronectin serum also demonstrated discriminatory capabilities. Immunofluorescent analysis of human fibroblasts grown in vitro demonstrated that all the monoclonal antibodies tested were reactive with pericellular fibronectin.
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PMID:Immunochemical analysis of fibronectin using monoclonal antibodies. 675 99

zeta-crystallin a novel NADPH: quinone oxidoreductase was purified from the cortex of the camel (Camelus dromedarius) lens to homogeneity by Sepharose CL-6B gel filtration column and 2', 5' ADP-Sepharose 4B affinity column chromatography in the presence of dithiothreitol. The purified zeta-crystallin has a molecular weight of 140 kDa, as determined by Superose 12 gel filtration column. SDS-PAGE showed a single polypeptide band of molecular weight 35 kDa, suggesting that the native enzyme is composed of four identical subunits. The isoelectric point of the enzyme was 7.6 on native polyacrylamide gel. The enzyme was purified 20-fold over homogenate with a specific activity of 26.0 Units/mg protein, and an overall recovery of 53%. This enzyme was NADPH specific and followed Michaelis-Menten kinetics. Km values for the reduction of 9,10-phenanthroquinone and oxidation of NADPH were 17 microM and 6.9 microM, respectively, at pH 7.8. The Vmax values of the enzyme for 9,10 phenanthroquinone and NADPH were 32 mumole min-1, mg-1 protein and 22.7 mumole min-1 mg-1 protein, respectively.
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PMID:Purification and characterization of zeta-crystallin from the camel lens. 748 2

Trypsin has been isolated and purified from the digestive glands of the slipper lobster, Thenus orientalis. It is a glycoprotein with a molecular mass of approximately 35 kDa as judged by both SDS-PAGE and gel filtration. The N-terminal amino acid sequence has strong homology to crustacean trypsins. This is confirmed by the cross-reaction of crustacean trypsins with antibodies to the T. orientalis enzyme. Despite a 40% identity with the bovine trypsin N-terminal sequence, there was no cross-reaction with the mammalian serine proteases. The optimum kcat and kcat/Km values for N-alpha-benzoylarginine-p-nitroanalide were 0.91 s-1 and 9.7 x 10(3) M-1 s-1, respectively, with this specificity constant being lower than those reported for other crustacean trypsins. Inhibition studies indicated the presence of serine and histidine at the active site and pKa of the catalytic histidine residue was found to be 5.7 in the free enzyme and 4.7 in the Michaelis complex.
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PMID:Isolation and characterization of a trypsin from the slipper lobster, Thenus orientalis (Lund). 750 56

The arginine and ornithine succinyltransferase from Pseudomonas aeruginosa, a bifunctional enzyme involved in the aerobic utilization of arginine and ornithine, has been purified to homogeneity. The apparent molecular mass of the native enzyme was 150 kDa by gel filtration and 140 kDa by polyacrylamide gel electrophoresis under non-denaturing conditions. After SDS/PAGE two subunits of 35 kDa and 37 kDa were evident, indicating that the enzyme is a heterotetramer. Microsequence analysis of the electroblotted protein bands gave two different but well-conserved N-terminal amino acid sequences. The L-arginine saturation curve followed Henri-Michaelis kinetics with an apparent Km value of 0.5 mM. The sigmoidal saturation curve for L-ornithine indicated allosteric behaviour. D-Arginine, a competitive inhibitor with respect to L-arginine, reduced L-ornithine cooperativity. In the presence of spermidine, the L-ornithine saturation curve became increasingly sigmoidal, the Hill coefficient shifting from 2.5 in the absence of the inhibitor, to 3.5 in the presence of 20 mM spermidine. The L-arginine analog, L-homoarginine, was also a substrate of the succinyltransferase, and the saturation of the enzyme by this substrate was also cooperative. All these data confirmed the allosteric nature of the enzyme. Moreover, a mutant growing faster on L-ornithine than the parent strain had a modified succinyltransferase with a reduced L-ornithine cooperativity. The fate of L-homoarginine was different depending on whether the succinyltransferase was induced or not; excreted succinylhomoarginine was found in cultures induced for the transferase activity whereas guanidinovalerate was excreted in non-induced cultures. The 'waste' of succinyl CoA, which could not be regenerated from the excreted succinylhomoarginine, explained the inhibition exerted by L-homoarginine on growth when ornithine or arginine was used as the growth medium.
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PMID:Purification and properties of a succinyltransferase from Pseudomonas aeruginosa specific for both arginine and ornithine. 752 19

This study deals with the acid phosphatase (AcPase) of the Kurloff body (KB), a large (10 microns diameter) periodic acid-Schiff-positive lysosomal inclusion body present in Kurloff cells (KC). KC AcPase were extracted, with similar yields, either with non-ionic detergent solution or after Dounce homogenization in low ionic strength buffer suggesting that they mainly correspond to hydrosoluble AcPase. After DEAE-cellulose chromatography of such crude Dounce-extracts, 97% of KC AcPase activity was recovered in the unbound glycoprotein fraction (peak I)1). The main protein content consisted of, as testified by SDS-PAGE analysis, major KC glycoproteins of 30-35 kDa. Thus, KC AcPase, and particularly sialoAcPase, may be assumed to correspond to these N-glycosylproteins among which the presence of alpha (2,6) sialoglycoproteins was previously established. Following electrophoresis on a 4-15% gradient native polyacrylamide gel or isoelectric focusing, the two size populations (200 kDa and 500 kDa) and up to 20 isoforms of KC AcPase were respectively detected by zymography in peak I. After Clostridium-derived sialidase digestion of peak I, the highly active bands observed at pH 3.5-5.2 disappeared. These zymographic patterns were similar to those obtained with crude extracts. After Concanavalin A (ConA)-Sepharose chromatography of peak I, the single ConA-bound glucosamine-labelled peak, eluted at 200 methyl-alpha-D-mannopyranose, contained the AcPase activity while the ConA-unbound peak was devoid of any acid phosphatase activity. After SDS-PAGE analysis, the ConA-bound fraction appeared to correspond only to a single broad protein band in the 30-35 kDa zone.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Relationship between the acid phosphatases of the Kurloff body and the major 30-35 kDa glycoproteins of the Kurloff cell. 754 9

Six basic proteins of 26 to 38 kDa with isoelectric points (pI) > or = 8.5 were abundant in proteins separated by two-dimensional SDS-PAGE from adult rat peritoneal mast cells (MC). One was identified previously as rat mast cell proteinase (RMCP) 1, a chymase of 26 to 28 kDa, pI > 9.0. Microsequence analyses showed that two polypeptides of about 29 and 30 kDa had NH2 terminal amino acid sequences homologous to mouse MC proteinase 5 (MCP-5), whereas the amino terminals of the 33, 35, and 36 kDa proteins were homologous to MC carboxypeptidase A (MC-CPA). Rabbit Abs produced against synthetic peptides of the identified NH2 terminal sequences were used in immunoblot studies. At least three proteins reacted with Abs to MC-CPA, whereas Abs to MCP-5 detected three adjacent polypeptides, rather than just the two identified by using microsequence analysis. Removal of oligosaccharide side chains using peptide:N-glycosidase F reduced the heterogeneity of each set of three polypeptides (MCP-5 and MC-CPA) to a band of each protein of a lower M(r). The serine proteinase inhibitor [3H]diisopropylfluorophosphate ([3H]DFP) bound to a proteinase of 30 to 35 kDa, which is probably MC tryptase (pI < or = 6.0). Immunoblot analysis of proteins from intestinal mucosal mast cells showed RMCP-2, but not RMCP-1, MCP-5, or MC-CPA. This is the first report of MCP-5 in the rat and of clearly distinguishable glycosylated forms of MC CPA. These proteinases appear to be restricted in their distribution to selected MC populations, but little is known about their functions.
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PMID:Proteinases of rat mast cells. Peritoneal but not intestinal mucosal mast cells express mast cell proteinase 5 and carboxypeptidase A. 759 1

The molecular biology of Mapuera virus was studied at both the protein and nucleic acid levels. Seven virus-encoded proteins were detected in infected Vero cells. The sizes and characteristics of each of the proteins determined from various radiolabelling experiments allowed preliminary identification of the proteins as the large (L; 190 kDa), haemagglutinin neuraminidase (HN; 74 kDa), nucleocapsid (N; 66 kDa), fusion (F0; 63 kDa), phosphoprotein (P; 49 kDa), matrix (M; 43 kDa) and non-structural (V; 35 kDa) proteins. Western blot analysis showed that the HN, N and P proteins were major antigens recognized in the mouse. A cDNA library of total virus-infected cellular mRNA was created and screening of the library resulted in the detection of cDNA sequences representing the N mRNA transcript of Mapuera virus. The N mRNA sequence determined from the clones was 1731 nt in length and contained an ORF that encoded 537 amino acids, the complete 3' untranslated region and part of the 5' non-coding region. The calculated M(r) of the N protein was 59 kDa, which is close to the 66 kDa protein observed by SDS-PAGE.
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PMID:Characterization of Mapuera virus: structure, proteins and nucleotide sequence of the gene encoding the nucleocapsid protein. 759 54

Membrane-bound fatty acyl-CoA reductase from the green alga Botryococcus braunii has been solubilized from the microsomal preparation by 0.1% octyl beta-glucoside and purified to near homogeneity by Blue A agarose and palmitoyl-CoA agarose affinity column chromatography. The molecular mass of the enzyme was estimated by SDS-PAGE to be 35 kDa. The enzyme generates fatty aldehyde by reduction of fatty acyl-CoA with NADH as the reductant. The N-terminal amino acid sequence of this protein that represents the first eucaryotic aldehyde-generating reductase to be purified shows high homology with the N-terminus of fatty acid reductase from bacteria.
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PMID:Solubilization and purification of aldehyde-generating fatty acyl-CoA reductase from green alga Botryococcus braunii. 764 95


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