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

This study tested the role of thyroxine in the regulation of the protein composition of rat parotid saliva. Thyro-parathyroidectomy was performed on two groups of rats, one of which subsequently received thyroxine replacement; the third group was sham-operated. Parotid saliva was collected on the eighth day after surgery, with pilocarpine and isoproterenol used as a secretory stimulus. The volume of saliva collected in 30 min from the thyro-parathyroidectomized rats was 55% less than that collected from sham-operated rats. In the thyro-parathyroidectomized rats, the protein concentration as measured by absorption at 215 nm was unaltered, but that measured by the Lowry procedure was 43% higher. Spectrophotometric scans of Coomassie Blue-stained gels following sodium dodecylsulfate polyacrylamide gel electrophoresis of the secreted proteins showed an 18% reduction in the proportion of protein attributable to amylase and a 43% reduction in proportion of acidic and basic proline-rich proteins following thyro-parathyroidectomy; deoxyribonuclease and two other major secretory proteins (Fraction I and Fraction V) were increased (38%, 20%, and 46%, respectively). These changes in flow rate, protein concentration by the Lowry assay, and protein composition were prevented by treatment of thyro-parathyroidectomized rats with thyroxine replacement and are in opposition to those changes we reported earlier for hyperthyroid rats. The results indicate that the flow of saliva as well as the synthesis of the various salivary proteins are influenced by thyroxine.
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PMID:Influence of thyroxine in the regulation of rat parotid salivary protein composition. 245 39

Chronic administration of the catecholamine-depleting agent, reserpine (0.5 mg/kg), resulted in a reduction in food intake after 3 days. To differentiate effects of the drug from those of reduced food intake a pair-fed group, whose daily caloric intake was restricted to the amount consumed by the reserpine-treated rats, was included. After 7 days, both the reserpine-treated and pair-fed control exhibited a marked reduction in the volume of saliva collected in a 30 min interval following a secretory stimulus compared to untreated ad libitum-fed controls, and the proportion of salivary proteins attributable to acidic and basic proline-rich proteins and to minor 1b protein were decreased whereas deoxyribonuclease was increased. For two of the salivary proteins (fractions I and V) changes for the reserpine-treated and pair-fed groups were different. Fraction I was reduced in both groups, but exhibited a greater decrease in the pair-fed than in the reserpine-treated, whereas fraction V was significantly increased only in the pair-fed group. Thus many of the salivary changes associated with reserpine treatment may have resulted from the change in feeding habits and not from reserpine treatment per se. The study demonstrates the importance of controlling for food intake under experimental circumstances which may lead to a marked change in daily feeding habits.
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PMID:Changes in rat parotid saliva protein composition following chronic reserpine treatment and their relation to inanition. 324 76

Forty-five kilobases of DNA, including the previously sequenced 2.2-kb inverted repeat region, located at the left termini of the 330-kb Chlorella virus PBCV-1 genome were sequenced and analyzed. Eighty-five complete open reading frames (ORFs) larger than 195 nucleotides were identified. Thirty-seven of the 85 ORFs, which are densely packed on both strands of the DNA, were considered major ORFs. Fifteen of the major ORFs have similarity to genes in the databases, including bacterial glycerophosphoryl diester phosphodiesterase, bacteriophage T4 endonuclease V, D-isomer specific 2-hydroxyacid dehydrogenases, and beta-alanine synthetase and bacterial nitrilases. Two major ORFs resemble the virus major capsid protein. Three major ORFs contain three or more ankyrin-like repeat elements and four ORFs encode proline-rich proteins.
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PMID:Analysis of 45 kb of DNA located at the left end of the chlorella virus PBCV-1 genome. 783 89

We tested the hypothesis that rats adapt to the iron absorption inhibitory effects of tea by modifying the expression of salivary proteins. Thirty-six weanling rats were allocated into 6 groups. Two control groups were fed a semipurified diet containing 20 mg Fe(2+)/kg diet. Two groups were fed spray dried green tea infusion mixed into the diet (28.6 g tea/kg diet) and 2 groups were fed the control diet with a twice daily gavage of a tea solution (0.25 g tea/mL). Saliva samples were collected in 3 groups (control, gavage, and oral) on day 8 (acute) and in the remaining groups on day 31 (chronic). Iron absorption was assessed using a (58)Fe(3+) tracer administered on day 1 (acute) and day 24 (chronic). 2D gel electrophoresis and mass spectrometry were used to assess the composition of the saliva proteome. There was no significant difference in iron absorption between the 3 groups on either day 1 or day 24. Salivary proline-rich proteins and submandibular gland secretory protein increased to a greater extent in the oral group than in the gavage group, when compared to control, within the same exposure time period. Amylase, chitinase, deoxyribonuclease, cysteine-rich secretory protein 1, and parotid secretory protein all decreased to a greater extent in the oral tea group, compared to the control, within the same exposure time period. Our results show that green tea did not decrease iron absorption in rats but it did have a marked effect on the saliva proteome when given orally.
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PMID:Green tea ingestion by rats does not affect iron absorption but does alter the composition of the saliva proteome. 2249 29