Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.25.1 (deoxyribonuclease)
 1,471 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The proteins of the secretory granules of the rat parotid gland were characterized by sodium dodecylsulfate gel electrophoresis, by chromatography of [3-H]proline-labeled proteins on DEAE-cellulose and by amino acid analysis. Sodium dodecylsulfate gel electrophoresis of the secretory granule content showed five principal proteins and a limited number of minor components. Only two of the principal bands could be identified as known secretory enzymes of the parotid gland. One was identified as the alpha-amylase and one as deoxyribonuclease. Peroxidase and ribonuclease form minor portions of the secretory proteins. The other three major proteins constitute, together, about 60% by weight, of the secretory granule content proteins. Of these, one which represents more than 30% of the total granule protein was found to contain uniquely high amounts of leucine residues (21 mole%). Another one of these principal proteins was relatively rich in cysteine residues (7 mole%). The fifth principal protein was found to contain high amounts of proline (28 mole%) glutamic acid (17 mole%) and glycine (18 mole%) residues. Its amino acid composition was very similar to that of the proline-se granules. This protein, however, differed from the "membranous" proline-rich proteins by several criteria. Two minor glycoproteins of the secretory granule content were also found to be rich in proline residues (37 mole%). As with the other proline-rich proteins of the granule, they contained no sulphur-containing amino acids, stained faintly pink with Coomassie Blue and were underestimated by the Lowry method. They differ however, from all the other proline-rich proteins of the granule by having a significantly higher content of threonine, less glycine (9 mole%) and much less glutamic acid (3 mole%). Of the principal proteins, only the deoxyribonuclease and the half-cystine-rich proteins were positively stained by periodic acid Schiff staining. The possible functions of the leucine-rich, the half cystine-rich and the various proline-rich proteins are discussed.
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PMID:The proteins of the content of the secretory granules of the rat parotid gland. 112 45

A variant of Staphylococcus aureus 44A HJD was isolated by serial growth in Trypticase soy broth to which 2 M serine had been added (wt/vol). Amino acid analysis of hydrolysates of purified mucopeptides from the variant showed that they contained 1.266 serine and 2.156 glycine residues per glutamic acid residue, compared with 0.174 serine and 3.144 glycine residues per glutamic acid residue in the mucopeptide of the parent strain. In addition to this alteration in the chemical composition of the mucopeptide, the variant lost many of the biochemical and cultural characteristics of the parent organism. The variant was not sensitive to the lytic action of lysostaphin and was non-phage-typable. Moreover, in vitro tests indicated that the organism was coagulase negative, did not produce gelatinase or deoxyribonuclease, and did not hemolyze sheep erythrocytes. Apparently due to the change in the serine content in the cell wall of the parent S. aureus strain, the organism had become "epidermidis-like" in its properties.
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PMID:In vitro incorporation of serine into the staphylococcal cell wall. 427 49

Cell walls were isolated by mechanical disruption of mid-log phase cells of Bacillus stearothermophilus NCA 1503-4R grown in Trypticase-yeast extract-fructose medium at 55 C. The cell walls were purified by treatment with sodium dodecyl sulfate (SDS) and incubation with deoxyribonuclease and trypsin. The cell wall peptidoglycan contained glucosamine, muramic acid, alpha, epsilon-diaminopimelic acid, and glutamic acid. Low amounts of glycine, galactosamine, serine, aspartic acid, lysine, and valine were also present. The relative mole ratios of glutamic acid-alpha, epsilon-diaminopimelic acid-glycine-alanine were 1.00:1.26:0.08:1.55. The cell walls were free from ribonucleic acid and deoxyribonucleic acid and contained less than 0.2% chloroform-methanol extractable lipid and 0.09 mumole of phosphorus per mg of cell wall. Teichoic acid was not detected in the cell walls of this organism. Cell walls isolated without treatment with SDS contained 7.5% chloroform-methanol extractable lipid, 0.24 mumole of phosphorus per mg of cell wall, and relatively high concentrations of all amino acids. These results suggest that the extracted lipid is not a cell wall component per se, but a contaminant from the lipoprotein cell membrane.
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PMID:Chemical composition of the cell walls of Bacillus stearothermophilus. 603 16

Isolated nuclei incubated with [14C]protein hydrolysate are shown to incorporate labelled amino acids into the acid-insoluble fraction. Purified chromatin and the complex of DNA with firmly bound proteins possess similar ability. The optimum pH of the reaction is 6.5-7.0, 2 mM MgCl2 stimulates incorporation, the temperature optimum is 37-40 degrees C. Chloramphenicol depresses incorporation by 70%, puromycin by 40%, cycloheximide does not affect the chromatin activity. Incorporation does not depend on the presence of ATP or GTP, and is substantially inhibited by deoxyribonuclease but not by ribonuclease treatment of chromatin or of the nuclei. Specific activity of firmly bound chromatin non-histone proteins is higher than that of labile bound ones; histones are not labelled. After pronase treatment of proteins radioactivity changes to an acid-soluble state. The molecular weight of isolated labelled polypeptides is about 6000 as shown by gel filtration and the analysis of NH2-terminal amino acids. Labelled polypeptides firmly bound to DNA consist of 7-10 amino acids. Specific activity of proteins firmly bound to DNA increases linearly with the time of incubation of chromatin with [14C]protein hydrolysate, the activity curve of labile bound non-histone proteins has a distinct sygmoid character. The polypeptide-synthesizing activity of rat liver chromatin increases between 9 h and 21 h after partial hepatectomy. Irradiation with 800 rads 30 min before the operation prevents activation of amino acid incorporation. From nine amino acids studied alanine, methionine, lysine, tyrosine and arginine are not incorporated in the system described. Glutamic acid is polymerized most effectively. Glutamine, asparagine and glycine are incorporated 7-8 times less. The data are given indicating that the incorporation is not random when an amino acid mixture is present. Preincubation of chromatin with NAD+ but not with its analogues increases the polypeptide-synthesizing activity of chromatin. The activation is prevented by thymidine and nicotinamide. Storage (18 h at 2-4 degrees C) brings about a complete loss of the polypeptide-synthesizing activity of chromatin. The ability of 'old' chromatin to incorporate amino acids can be restored by preincubating it with NAD+. Storage of chromatin in the presence of 5 mM adenosine 3',5'-monophosphate (cAMP) does not result in decrease of the polypeptide-synthesizing activity. It is assumed that poly-(ADP-ribose) is the energy source for amino acid activation in the system described.
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PMID:Polypeptide-synthesizing activity of eukaryotic chromatin. Properties, dependence on poly(ADP-ribose) and connection with the cell cycle. 737 37

Syringacin 4-A, a bacteriocin produced by Pseudomonas syrinagae 4-A, was obtained by induction with ultraviolet irradiation or mitomycin C. Approximately 1,000-fold purification of the bacteriocin was achieved by manganous chloride precipitation, differential centrifugation, and chromatography on hydroxyapatite columns. The purified syngacin was homogeneous on hydroxyapatite columns and sucrose density gradients; it also sedimented as a single entity in the analytical ultracentrifuge. The buoyant density of purified syringacin in cesium chloride was 1.294 g/ml. The sedimentation coefficient was calculated as 120S, and the diffusion coefficient was 6.49 x 10(-8) cm(2)/s. The molecular weight was calculated as 1.6 x 10(7) from physical data and 1.7 x 10(7) from biological data. The syringacin was composed of about 88.4% protein, 8.5% arabinose, 2.2% galacturonic acid, and 0.7% glucosamine. Amino acid analysis indicated a predominance of leucine (12.1%), aspartic acid (12.2%), and glutamic acid (12.7%). The ultraviolet spectrum showed a maximum absorbance peak at 276 nm. The syringacin was heat and alcohol sensitive, but resistant to trypsin, chymotrypsin, carboxypeptidase, Pronase, protease, lysozyme, steapsin, deoxyribonuclease, and ribonuclease. Maximum pH stability was between 5 and 8. Crude bacteriocin was stable at room temperature for at least a year, and purified material was stable for at least 3 months at 4 C.
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PMID:Purification and characterization of syringacin 4-A, a bacteriocin from pseudomonas syringae 4-A. 1582 74