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Your search keyword '"Nakamura, Ryo"' showing total 87 results
Start Over Author "Nakamura, Ryo" Publication Year Range More than 50 years ago
87 results on '"Nakamura, Ryo"'

4. Isolation and Characterization of β-N-Acetylglucosaminidase from Human Parotid Saliva.

Author

TATSUO WATANABE, NAKAMURA, RYO, IWAMOTO, YOSHIFUMI, and TSUNEMITSU, AKIRA

Subjects
ENZYME kinetics, SALIVA analysis, PAROTID glands, HYDROLYSIS, GEL electrophoresis, DIETHYLAMINOETHANOL, ASPERGILLUS
Abstract

Beta-N-acetylglucosaminidase in human parotid saliva was separated into two subfractions by diethylaminoethanol cellulose column chromatography. One subtraction of the enzyme was isolated and purified. Disk electrophoresis showed that the purified enzyme was homogeneous. The molecular weight of this enzyme was estimated to be about 153,000 by gel filtration and dodecyl sulfate polyacrylamide gel electrophoresis. N-acetyl-β-galactosaminides also were hydrolyzed by this enzyme at the same site. [ABSTRACT FROM AUTHOR]

Published
1973
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5. Heterogeneity of Peroxidase Related to Antibacterial Activity in Human Parotid Saliva.

Author

IWAMOTO, YOSHIFUMI, NAKAMURA, RYO, WATANABE, TATSUO, and TSUNEMITSU, AKIRA

Subjects
PEROXIDASE, SALIVA microbiology, ANTIBACTERIAL agents, HETEROGENEITY, ISOELECTRIC focusing, CHROMATOGRAPHIC analysis, LACTOBACILLUS casei
Abstract

The peroxidase that is related to the thiocyanate-peroxidase-hydrogen peroxide anti-bacterial system in human parotid saliva was separated into three sub fractions by diethylaminoethanol (DEAE)-cellulose column chromatography. Heterogeneity was confirmed by isoelectric focusing. Three subtractions contributed to the inhibition of the growth of Lactobacillus casei ATCC 7469. [ABSTRACT FROM AUTHOR]

Published
1972
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6. Nucleotidase Activity of the Purified Acid Phosphomonoesterase from Human Parotid Saliva.

Author

NAKAMURA, RYO, WATANABE, TATSUO, IWAMOTO, YOSHIFUMI, and TSUNEMITSU, AKIRA

Subjects
ACID phosphatase, NUCLEOTIDES, SODIUM fluoride, SALIVA, PAROTID glands, HYDROGEN-ion concentration, MERCURY
Abstract

Purified acid phosphomonoesterase from human parotid saliva has been characterized as an acid nucleotidase of broad specificity. The enzyme exhibited a pH optimum at 5.8 with 5'-AMP and was not metal dependent. Activity was inhibited greatly by mercuric ions, sodium fluoride, and sodium tartrate. The tartrate inhibition was competitive. [ABSTRACT FROM AUTHOR]

Published
1971
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7. Purification and Amino Acid Analysis of Human Parotid Saliva Lysozyme.

Author

IWAMOTO, YOSHIFUMI, NAKAMURA, RYO, WATANABE, TATSUO, and TSUNEMITSU, AKIRA

Subjects
AMINO acid analysis, SALIVA analysis, LYSOZYMES, PAROTID glands, ENZYME kinetics, TRYPTOPHAN
Abstract

Lysozyme from human parotid saliva was purified to the point where it was judged, by the criteria of ultracentrifugation and disk electrophoresis, to be homogeneous. The parotid lysozyme had a specific activity 3.5 times greater than that of hen egg-white lysozyme and a composition that was different, especially in regard to tyrosine, serine, and glutamic acid content. The molecular weight was determined to be around 14,300. When tryptophan residues were modified with N-bromosuccinamide, no lytic activity was found, which indicates that the tryptophan residues may play an important role in the maintenance of the parotid lysozyme activity. [ABSTRACT FROM AUTHOR]

Published
1970
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8. Purification and Properties of Acid Phosphomonoesterase from Human Parotid Saliva.

Author

NAKAMURA, RYO, WATANABE, TATSUO, IWAMOTO, YOSHIFUMI, and TSUNEMITSU, AKIRA

Subjects
SALIVA, BODY fluids, EXOCRINE secretions, PAROTID glands, DENTAL research
Abstract

Acid phosphomonoesterase was separated from human parotid saliva and purified. The purified enzyme was proved homogeneous on sedimentation and disk electrophoresis. The optimal pH of the enzyme was 3.3. The enzyme had no substrate specificity for phosphomonoesters and its activity was inhibited by SnF2 or NaF. [ABSTRACT FROM AUTHOR]

Published
1970
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9. Study of CoQ10-Enzymes in Gingiva from Patients with Periodontal Disease and Evidence for a Deficiency of Coenzyme Q10*

Author

Nakamura, Ryo, Littarru, Gian Paolo, Folkers, Karl, and Wilkinson, Edward G.

Abstract

The specific activities of both the succinate dehydrogenase-coenzyme Q10reductase and the DPNH-cytochrome creductase [NADH:(acceptor)oxidoreductase, EC 1.6.99.3] were determined in mitochondria from 40 diseased gingival biopsies from patients with periodontal disease and from 24 control biopsies from nondiseased areas (clinically evaluated) of gingival tissues from the same mouths of the patients from whom the diseased gingival tissues were taken. The control tissue was taken during normal surgical procedures, such as for gingival recontouring and tuberosity removal.The diseased gingival biopsies showed a mean specific activity for the succinate dehydrogenase-coenzyme Q10reductase which was higher (P< 0.02) than that of the control biopsies, and which increased (P< 0.01) when the assays utilized exogenous coenzyme Q3, and corresponded to an average deficiency of coenzyme Q10-enzyme activity of 35%. About 60% of the 40 diseased gingival tissues showed a deficiency of coenzyme Q10at its site in this succinate-coenzyme Q10enzyme. Of the 24 control tissues, 20% showed deficiencies of coenzyme Q10. As a group, the control tissues showed no deficiency of coenzyme Q10.No deficiency of coenzyme Q10at its site in DPNH-cytochrome creductase was observed for either the control or diseased gingival tissues, as groups or individually.

Published
1974
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10. Deficiency of Coenzyme Q10in Gingival Tissue from Patients with Periodontal Disease

Author

Littarru, Gian Paolo, Nakamura, Ryo, Ho, Lester, Folkers, Karl, and Kuzell, William C.

Abstract

The specific activities of the succinate dehydrogenase-coenzyme Q10reductase in gingival tissue from patients with periodontal disease have been compared with the corresponding specific activities of normal human periodontal tissue. The gingival biopsies from patients having diseased periodontal tissue showed a deficiency of coenzyme Q10, in contrast to those of the normal periodontal tissue which showed no deficiency. The presence or absence of a deficiency of coenzyme Q10in the succinate-coenzyme Q10enzyme system is appraised by determining the specific activity in the absence and again in the presence of exogenous coenzyme Q3. An increase in specific activity of this mitochondrial enzyme system in the presence of exogenous coenzyme Q3reflects the mitochondrial deficiency of coenzyme Q10. Such increases ranged from 38-120% and averaged 81% for the individuals with periodontal disease, and were highly significant statistically.These data correlate with clinical studies in Japan that have indicated a therapeutic benefit of the administration of coenzyme Q7to many patients with severe and destructive periodontal disease and with the benefit of administration of hexahydrocoenzyme Q4to one such patient in the current work.

Published
1971
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