THE EFFECT OF L-ASCORBIC ACID ON MYROSINASE ACTIVITY
The addition of 10-2 to 10-3M L-ascorbic acid to the reaction medium was found to greatly promote the white mustard myrosinase activity under the condition (pH 6.4), producing neither white turbidity nor hydrogen sulfide. The amount of the white turbidity and hydrogen sulfide produced on addition of...
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| Published in | Journal of vitaminology Vol. 10; no. 1; pp. 44 - 54 |
|---|---|
| Main Authors | , |
| Format | Journal Article |
| Language | English |
| Published |
Japan
THE VITAMIN SOCIETY OF JAPAN
01.01.1964
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0022-5398 |
| DOI | 10.5925/jnsv1954.10.44 |
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| Abstract | The addition of 10-2 to 10-3M L-ascorbic acid to the reaction medium was found to greatly promote the white mustard myrosinase activity under the condition (pH 6.4), producing neither white turbidity nor hydrogen sulfide. The amount of the white turbidity and hydrogen sulfide produced on addition of ascorbic acid to the reaction mixture of myrosinase and sinigrin increased with the decrease of the pH value of the medium. Any of those materials was produced in a larger amount in the case of white mustard enzyme than in the case of mold enzyme. The material producing white turbidity was found to be composed mainly of protein. It may be concluded that ascobic acid is a specific activator of myrosinase. |
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| AbstractList | The addition of 10-2 to 10-3M L-ascorbic acid to the reaction medium was found to greatly promote the white mustard myrosinase activity under the condition (pH 6.4), producing neither white turbidity nor hydrogen sulfide. The amount of the white turbidity and hydrogen sulfide produced on addition of ascorbic acid to the reaction mixture of myrosinase and sinigrin increased with the decrease of the pH value of the medium. Any of those materials was produced in a larger amount in the case of white mustard enzyme than in the case of mold enzyme. The material producing white turbidity was found to be composed mainly of protein. It may be concluded that ascobic acid is a specific activator of myrosinase. |
| Author | KOJIMA, MISAO TAMIYA, KEIKO |
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| Keywords | ENZYME INHIBITORS EXPERIMENTAL LAB STUDY CYSTEINE HYDROGEN-ION CONCENTRATION COENZYMES SPECTRUM ANALYSIS ASCORBIC ACID MUSTARD ASPERGILLUS SULFATASES GALLIC ACID GLUTATHIONE AMYLASE CHEMISTRY CHLOROMERCURIBENZOATES |
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| References | 9. Gaines, R. D., and Goering, K. J., Biochem. Biophys. Res. Comm. 2, 207 (1960). 15. Kojima, M., and Yazaki, M., J. Fer. Tech. (Japan) 33, 392 (1955). 16. Nagashima, Z., J. Agr. Chem. Soc. (Japan) 31, 514 (1957). 2. Ettlinger, M. G., and Lundeen, A. J., J. Amer. Chem. Soc. 78, 4172 (1956). 4. Nagashima. Z.. and Uchiyama, M., J. Agr. Chem. Soc. (Japan) 33, 980 (1959). 11. Braecke, J., J. Pharm. Belg. 10, 481 (1928). 3. Nagashima, Z., and Uchiyama, M., Bull. Agr. Chem. Soc. Japan 23, 555 (1959). 10. Nagashima, Z., and Uchiyama, M.. J. Agr. Chem. Soc. (Japan) 33, 484 (1959). 1. Neuberg, C., and Schoenbech, O., Naturwissenschaften 21, 404 (1933). 14. Andre, E., and Carboueres, M. D., Compt. rend. 240, 1468 (1955). 14. Andre, E., and Carboueres, M. D., Compt. rend. 244, 3080 (1957). 1. Neuberg, C., and Schoenbech, O., Biochem. Z. 265, 223 (1933). 6. Ettlinger, M. G., Dateo, Jr., G. P., Harrison, B. M., Babry, T. J., and Thomson, C. P., Proc. Natl. Acad. Sci. U.S. 47, 1875, 1961). 17. Summer, J. B., J. Biol. Chem. 65, 393 (1932). 2. Ettlinger, M. G., and Lundeen, A. J., J. Amer. Chem. Soc. 79, 1764 (1957). 18. Jensen, E. V., Science 130, 139 (1959). 7. Schwimmer, S., Acta Chem. Scnd. 15, 535 (1961) 8. Schwimmer, S., Acta Chem. Scnd. 14, 1439 (1960). 3. Nagashima, Z., and Uchiyama, M., J. Agr. Che. Soc. (Japan) 33, 1143 (1959). 13. St. Lorant, I., Z. Physiol. Chem. 185, 245 (1929). 5. Nagashima, Z., Uchiyama, M., and Nishioka, S., J. Agr. Chem. Soc. (Japan) 33, 723 (1959). 12. Nagashima, Z., and Nakagawa, M., J. Agr. Chem. Soc. (Japan). 31, 416 (1957). |
| References_xml | – reference: 5. Nagashima, Z., Uchiyama, M., and Nishioka, S., J. Agr. Chem. Soc. (Japan) 33, 723 (1959). – reference: 9. Gaines, R. D., and Goering, K. J., Biochem. Biophys. Res. Comm. 2, 207 (1960). – reference: 3. Nagashima, Z., and Uchiyama, M., Bull. Agr. Chem. Soc. Japan 23, 555 (1959). – reference: 1. Neuberg, C., and Schoenbech, O., Naturwissenschaften 21, 404 (1933). – reference: 17. Summer, J. B., J. Biol. Chem. 65, 393 (1932). – reference: 16. Nagashima, Z., J. Agr. Chem. Soc. (Japan) 31, 514 (1957). – reference: 3. Nagashima, Z., and Uchiyama, M., J. Agr. Che. Soc. (Japan) 33, 1143 (1959). – reference: 8. Schwimmer, S., Acta Chem. Scnd. 14, 1439 (1960). – reference: 7. Schwimmer, S., Acta Chem. Scnd. 15, 535 (1961) – reference: 18. Jensen, E. V., Science 130, 139 (1959). – reference: 10. Nagashima, Z., and Uchiyama, M.. J. Agr. Chem. Soc. (Japan) 33, 484 (1959). – reference: 12. Nagashima, Z., and Nakagawa, M., J. Agr. Chem. Soc. (Japan). 31, 416 (1957). – reference: 11. Braecke, J., J. Pharm. Belg. 10, 481 (1928). – reference: 2. Ettlinger, M. G., and Lundeen, A. J., J. Amer. Chem. Soc. 79, 1764 (1957). – reference: 14. Andre, E., and Carboueres, M. D., Compt. rend. 244, 3080 (1957). – reference: 15. Kojima, M., and Yazaki, M., J. Fer. Tech. (Japan) 33, 392 (1955). – reference: 14. Andre, E., and Carboueres, M. D., Compt. rend. 240, 1468 (1955). – reference: 13. St. Lorant, I., Z. Physiol. Chem. 185, 245 (1929). – reference: 1. Neuberg, C., and Schoenbech, O., Biochem. Z. 265, 223 (1933). – reference: 2. Ettlinger, M. G., and Lundeen, A. J., J. Amer. Chem. Soc. 78, 4172 (1956). – reference: 4. Nagashima. Z.. and Uchiyama, M., J. Agr. Chem. Soc. (Japan) 33, 980 (1959). – reference: 6. Ettlinger, M. G., Dateo, Jr., G. P., Harrison, B. M., Babry, T. J., and Thomson, C. P., Proc. Natl. Acad. Sci. U.S. 47, 1875, 1961). |
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| SubjectTerms | Amylases Ascorbic Acid Aspergillus Chemical Phenomena Chemistry Chloromercuribenzoates Coenzymes Cysteine Enzyme Inhibitors Gallic Acid Glutathione Glycoside Hydrolases Hydrogen-Ion Concentration Mustard Plant OldMedline Spectrum Analysis Sulfatases |
| Title | THE EFFECT OF L-ASCORBIC ACID ON MYROSINASE ACTIVITY |
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