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)

A new enzyme, N-alkylglycine oxidase, was isolated from a soil mold, Cladosporium sp. G-10. This protein, which was purified to near homogeneity by ammonium sulfate precipitation followed by successive column chromatography on phenyl-Sepharose, DEAE-Sepharose and Sephadex G-200, was a single polypeptide with a molecular mass of 52,000. In the presence of O2 and H2O, this enzyme acted on some N-alkylglycine derivatives, such as N epsilon-carboxymethyllysine, N-carboxymethyl-6-aminocaproic acid, sarcosine and N-ethylglycine, and produced corresponding N-alkylamine, glyoxylic acid and H2O2. This enzyme had optimum activity at 30 degrees C, pH 8-10, and was most inhibited by ZnSO4, pCMB, iodoacetic acid, and SDS.
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PMID:Purification and characterization of a new enzyme, N-alkylglycine oxidase from Cladosporium sp. G-10. 998 29

Aminopeptidase H was isolated and purified from fresh skeletal muscle of the lizard Agama stellio stellio by ammonium sulfate fractionation and successive chromatographies on DEAE-cellulose, Ultrogel AcA-34, activated thiol-Sepharose 4B, phenyl-Sepharose CL-4B, and DEAE-cellulose again. This is the first report of the isolation of aminopeptidase H from a reptile. The purified enzyme migrated as a single band on SDS-PAGE. The molecular weight of the enzyme was 48 kD by SDS-PAGE and 384 kD on Ultrogel AcA-34 column chromatography. The optimum pH for hydrolysis of L-leucine beta-naphthylamide (Leu-Nap) was 7.8. The Km values for the hydrolysis of Leu-Nap and Nalpha-benzoyl-DL-arginine beta-naphthylamide (BzArg-Nap) were 0.48 and 0.99 mM, respectively. These activities were strongly inhibited by iodoacetic acid and leupeptin but were not affected by EDTA, pepstatin, bestatin, or phenylmethylsulfonyl fluoride. The enzyme has been shown not to hydrolyze proteins such as hemoglobin, BSA, myofibrillar proteins, and sarcoplasmic proteins.
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PMID:Isolation, purification, and properties of aminopeptidase H from skeletal muscle of the lizard Agama stellio stellio. 1018 16

As a preliminary study for the explanation of pathobiology of Neodiplostomum seoulense infection, a 54 kDa protease was purified from the crude extract of adult worms by sequential chromatographic methods. The crude extract was subjected to DEAE-Sepharose Fast Flow column, and protein was eluted using 25 mM Tris-HCl (pH 7.4) containing 0.05, 0.1, 0.2 and 0.4 M NaCl in stepwise elution. The 0.2 M NaCl fraction was further purified by Q-Sepharose chromatography and protein was eluted using 20 mM sodium acetate (pH 6.4) containing 0.05, 0.1, 0.2 and 0.3 M NaCl, respectively. The 0.1M NaCl fraction showed a single protein band on SDS-PAGE carried out on a 7.5-15% gradient gel. The proteolytic activities of the purified enzyme were specifically inhibited by L-trans-epoxy-succinylleucylamide (4-guanidino) butane (E-64) and iodoacetic acid. The enzyme, cysteine protease, showed the maximum proteolytic activity at pH 6.0 in 0.1 M buffer, and degraded extracellular matrix proteins such as collagen and fibronectin with different activities. It is suggested that the cysteine protease may play a role in the nutrient uptake of N. seoulense from the host intestine.
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PMID:A 54 kDa cysteine protease purified from the crude extract of Neodiplostomum seoulense adult worms. 1018 82

The bleeding syndrome produced by contact with the Lonomia achelous caterpillars is characterized by a decrease of fibrinogen, factor XIII, plasminogen, and factor V with normal platelets. In this study, we report the effect of crude hemolymph and some semipurified chromatographic fractions on human factor V. Incubation of factor V with crude hemolymph resulted in an increase in procoagulant activity, followed by a subsequent decline in factor V activity. Identical results were obtained with fraction I, whereas with fraction II there was only a decrease in activity reaching its minimum at 30 minutes. fraction III did not modify the activity of factor V. All concentrations of fraction I tested produced an initial rise and subsequent fall in activity. However, at lower relative concentrations of fraction I, more sustained increases in activity were observed. The activator and inactivator activities present in fraction I show differences in temperature and pH stability, susceptibility to different inhibitors, and in SDS/PAGE pattern. The factor V activator is a thermostable protein, with maximum activity at acid pH and is inhibited by o-phenantroline, EDTA, and EGTA, while the factor V inactivator is thermolabile, presents maximum activity at basic pH, precipitates at pH 5.0, and is completely inhibited by iodoacetic acid and TLCK. It is partially blocked by diisopropyl fluorophosphate, phenylmethylsulfonyl fluoride, and p-chloromercuribenzoic acid. These results suggest that the activator should be a metallo-proteinase, while the inactivator is a serine or cysteine proteinase with a serine, histidine, or cysteine residue in the active site.
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PMID:The action of Lonomia achelous caterpillars venom on human factor V. 1070 38

A serine protease from mite faecal extract, Dermatophagoides farinae, was purified using DEAE-Sephacel anion exchange chromatography and Superdex 75 pg gel chromatography. The molecular weight of this protease was 34 kD on SDS-PAGE under reducing conditions. The optimal pH and temperature of the protease were 8.0 and 47 degrees C, respectively. In addition, this protease cleaved arginyl or lysyl residue containing substrates selectively and was only inhibited by aprotinin, FUT-175, and soy bean trypsin inhibitor and not by chymostatin, E-64 and iodoacetic acid. These results show that our purified serine protease belongs to the trypsin-type. Purified trypsin-like protease was shown to be allergenic by enzyme-linked immunosorbent assay. Antigenicity of trypsin-like protease was completely different from those of Der f I and Der f II. Both, 20 N-terminal amino acid sequence and amino acid compositions of the purified protease were very similar to those of Der f III. Good similarities were found between trypsin-like protease and Der f III concerning physicochemical properties such as molecular weight on SDS-PAGE and ammonium sulphate solubility. Summarizing the above data, it can be concluded that a trypsin-like protease from mite faecal extract is actually the Der f III allergen and that it may be involved in the digestive process of the mite as it was found not in mite body but in mite faeces.
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PMID:Trypsin-like protease of mites: purification and characterization of trypsin-like protease from mite faecal extract Dermatophagoides farinae. Relationship between trypsin-like protease and Der f III. 1077 9

A protease from the culture supernatant of Bacteroides gingivalis 381, which hydrolyzes the chromogenic substrate Na-benzoyl-DL-arginine-p-nitroanilide (BAPNA), was partially purified by ammonium sulfate precipitation, gel filtration, and anion exchange chromatography. The molecular weight of this protease was determined by SDS-PAGE to be ca. 49,000. The optimum pH was around 7.6. The protease was stable at neutral pH and up to 40 degrees C. The isoelectric point was 4.9. The enzyme activity was enhanced by dithiothreitol, L-cysteine, and 2-mercaptoethanol and inhibited by p-chloromercuribenzoic acid, N-ethylmaleimide, and iodoacetic acid.
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PMID:Purification and characterization of a thiol-protease from Bacteroides gingivalis strain 381. 1087 Apr 72

Peptide fragments, isolated from proteolytic cleavage of thyroglobulin at specific sites, were examined for the iodination of tyrosine residues. The 50 kDa polypeptide, which was prepared from digestion of bovine thyroglobulin and continuous preparative SDS-PAGE, was subjected to reduction with DTT and alkylation with iodoacetic acid to generate S-carboxymethylated peptide derivative, which was further hydrolysed by endoproteinase-Asp N. Peptide products were separated by RP-HPLC, and each fraction was analyzed by LC/ ESI-MS and MALDI-MS analyses. Based on the specificity of endoproteinase Asp-N and the mass spectra data, a peptide fragment turned out to correspond to a peptide, DALGCVKCPEGSYFQ (1438-1452), characterized by the presence of a thioredoxin box (CVKC) and a tyrosine residue. In addition, another peptide fragment (1453-1465) containing a thioredoxin box (CIPC) and a tyrosine residue was also observed. However, any evidence of iodination of the tyrosine residue present in these peptides was not provided. Meanwhile, tyrosine residues in the peptides, DVEEALAGKYLAGRFA (1366-1381) and DYSGLLLAFQVFLL (1290-1303) were found to be iodinated; mono- or diiodinated tyrosine residues, characteristic of a hormogenic site, existed in both peptides. In addition, the tyrosine residue in the peptide (1218-1252), corresponding to a hormonogenic site was also iodinated. Thus, there was a sharp difference of the susceptibility to oxidative iodination between the tyrosine residue in a hormonogenic site and that in a thioredoxin region. From these results, it is suggested that polypeptide region adjacent to tyrosine residues may govern the susceptibility of tyrosine to oxidative iodination.
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PMID:Difference in susceptibility of tyrosine residue to oxidative lodination between a thioredoxin box region and a hormonogenic region. 1169 49

Alpha-Amylase (EC 3.2.1.1) was purified from the muscle and intestine of the parasitic helminth of pigs Ascaris suum. The enzymes from the two sources differed in their properties. Isoelectric focusing revealed one form of a-amylase from muscles with pl of 5.0, and two forms of amylase from intestine with pI of 4.7 and 4.5. SDS/PAGE suggested a molecular mass of 83 kDa and 73 kDa for isoenzymes of a-amylases from intestine and 59 kDa for the muscle enzyme. Alpha-Amylase from intestine showed maximum activity at pH 7.4, and the enzyme from muscle at pH 8.2. The muscle enzyme was more thermostabile than the intestinal alpha-amylase. Both the muscle and intestine amylase lost half of its activity after 15 min at 70 degrees C and 50 degrees C, respectively. The Km values were: for muscle amylase 0.22 microg/ml glycogen and 3.33 microg/ml starch, and for intestine amylase 1.77 microg/ml glycogen and 0.48 microg/ml starch. Both amylases were activated by Ca2+ and inhibited by EDTA, iodoacetic acid, p-chloromercuribenzoate and the inhibitor of a-amylase from wheat. No significant differences were found between the properties of a-amylases from parasites and from their hosts.
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PMID:Purification and characterization of alpha-amylases from the intestine and muscle of ascaris suum (Nematoda). 1183 85

Glutathione peroxidase (EC 1.11.1.9) present in the liver of Japanese sea bass (Lateolabrax japonicus) was extracted and purified by phenyl-toyopearl 650M, butyl-toyopearl 650M and DEAE-toyopearl 650M column chromatography. The molecular weight of the enzyme was estimated to be about 70 kDa by gel filtration by toyopearl HW-55F. On SDS-PAGE, this enzyme was composed of two identical subunits with 35 kDa and was a dimer. This enzyme was a typical SH-enzyme that was inhibited by iodoacetic acid, PCMB, DTNB, and Hg.
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PMID:Glutathione peroxidase from the liver of Japanese sea bass Lateolabrax japonicus. 1192 31

O-Acetyl-L-serine sulfhydrylase (EC 4.2.99.8) was first purified from an extremely thermophilic bacterium, Thermus thermophilus HB8, in order to ascertain that it is responsible for the cysteine synthesis in this organism cultured with either sulfate or methionine given as a sole sulfur source. Polyacrylamide gel electrophoreses both with and without SDS found high purity of the enzyme preparations finally obtained, through ammonium sulfate fractionation, ion exchange chromatography, gel filtration, and hydrophobic chromatography (or affinity chromatography). The enzyme activity formed only one elution curve in each of the four different chromatographies, strongly suggesting the presence of only one enzyme species in this organism. Molecular masses of 34,000 and 68,000 were estimated for dissociated subunit and the native enzyme, respectively, suggesting a homodimeric structure. The enzyme was stable at 70 degrees C at pH 7.8 for 60 min, and more than 90% of the activity was retained after incubation of its solution at 80 degrees C with 10 mm dithiothreitol. The enzyme was also quite stable at pH 8-12 (50 degrees C, 30 min). It had an apparent Km of 4.8 mM for O-acetyl-L-serine (with 1 mM sulfide) and a Vmax of 435 micromol/min/mg of protein. The apparent Km for sulfide was approximately 50 microM (with 20 mM acetylserine), suggesting that the enzyme can react with sulfide liberated very slowly from methionine. The absorption spectrum of the holo-enzyme and inhibition of the activity by carbonyl reagents suggested the presence of pyridoxal 5'-phosphate as a cofactor. The apo-enzyme showed an apparent Km of 29 microM for the cofactor at pH 8. Monoiodoacetic acid (1 mM) almost completely inactivated the enzyme. The meaning of a very high enzyme content in the cell is discussed.
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PMID:Cysteine synthase of an extremely thermophilic bacterium, Thermus thermophilus HB8. 1200 48


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