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• W2017332590 abstract "Physiologia PlantarumVolume 18, Issue 3 p. 604-625 An α-Amylase from Tobacco Crown-Gall Tissue Cultures I. Purification and Some Properties of the Enzyme. Pattern of α-Amylase Isoenzymes in Different Tobacco Tissues E. M. J. Jaspars, E. M. J. Jaspars Department of Biochemistry. University of Leydon The NetherlandsSearch for more papers by this authorH. Veldstra, H. Veldstra Department of Biochemistry. University of Leydon The NetherlandsSearch for more papers by this author E. M. J. Jaspars, E. M. J. Jaspars Department of Biochemistry. University of Leydon The NetherlandsSearch for more papers by this authorH. Veldstra, H. Veldstra Department of Biochemistry. University of Leydon The NetherlandsSearch for more papers by this author First published: July 1965 https://doi.org/10.1111/j.1399-3054.1965.tb06922.xCitations: 14AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 Balls, A. K. & Marlin, L. F.: Amylase activity of mosaic tobacco. Enzymologia 5: 233–238. 1938–39. 2 Balls, A. K. Walden, M. K. & Thompson, R. R.: A crystalline β-amylase from sweet potatoes. J. Biol. Chem. L73: 9–19. 1948. 3 Bernfeld, P.: Enzymes of starch degradation and synthesis. Adv. Enzym. 12: 379–428. 1951. 4 Bonavita, V., Ponte, F. & Amore, G.: Lactate dehydrogenase isozymes in the developing rat brain. Nature 196: 576–577. 1962. 5 Brakke, M. K. & Nickell, L. G.: Seeretion of α-amylase by Rumex virus tumors in vitro. Properties and assay. Arch. Biochem. Biophys. 32: 28–41. 1951. 6 Braun, A. C.: A demonstration of the recovery of the crown-gall tumor cell with the use of complex tumors of single-cell origin. Proc. Natl. Acad. Sci. (U.S.) 45: 932–938. 1959. 7 Bünning, E.: Untersuchungen über den physiologischen Mechanismus der endogenen Tagesrhythmik bei Pflanzen. Z. Bot. 37: 433–486. 1942. 8 Cahn, R. P., Kaplan, N. O., Levine, L. & Zwilling, K.: Nature and development of lactic dehtydrogenases. Science 136: 962–969. 1962. 9 Carter, D. V. & Sykes, G.: The assay of enzyme activity by the plate diffusion technique. J. Pharm. Pharmacol. 13 supp: 195-T–199-T. 1961. 10 Dube, S. K. & Nordin, P.: Isolation and properties of sorghum α-amylase. Arch. Biochem. Biophys. 94: 121–127. 1961. 11 Ehrenberg, M.: Beziehungen zwisehen Fermttätigkeit und Blattbewegung bei Phaseolus multiflores unter verschiedenen photoperiodischen Bedingungen, — Planta 38: 244–279. 1950. 12 Fine, I. H., Kaplan, N. O. & Kuftinec, D.: Developmental changes of mammalian lactic dehydrogenases. Biochemistry 2: 116–121. 1963. 13 Finn, H. K.: Theory of agar diffusion methods for bioassay. Anal. Chem. 31: 975–977. 1959. 14 Fischer, E. H. & Haselbach. C. H.: Sur les enzymes amylolytiqies. XVII. Contribution à I'étude de I'α-amylase de malt, — Helv. Chim. Acta 34: 325–334. 1951. 15 Fischer, E. H. & Stein, E. A.: α-Amylases. — In Boyer. P. D., Lardy, H. & Myrbäck, K.: The Enzymes 4: 313–343. 2nd ed. Acad. Press, New York and London . 1960. 16 Fondy, T. P., Pesce, A., Freedberp, I., Stolzenbach, F. & Kapln, N. O.: The comparative enzymology of lactic dehydrogenases. II. Properties of the crystalline HM3 hybrid from chicken muscle and of H2M2 hybrid and H4 enzyme from chicken liver. Biochemistry 3: 522–530. 1964. 17 Frankenburg, W. G.: Chemical changes in the harvested tobacco leaf. Part 1. Chemical and enzymic conversion during the curing process. Adv. Enzymol. 6: 309–387 1946. 18 French, D.: β-Amylases. — In Boyer, P. D., Lardy, H. A. Myrbäck, K.: The Enzymes 4: 345–368. 2nd ed. Acad. Press. New York and London . 1960. 19 Fukumoto, J. & Tsujisaka, Y.: Purification and crystallization of β-amylase from soybeans. Science and Ind. Japan 28: 282–287. 1954. 20 Gautheret, R. L.: La culture des tissus végétaux. — Masson. Paris . 1959. 21 Hjertén, S.: Agarose as an anticonvection agent in zone electrophoresis. Biochim. Biophys. Acta 53: 514–517. 1961. 22 Holmberg, O.: Über die Adsorption von α-Amylase aus Malz an Stärke. Biochem. Z. 258: 134–140 1933. 23 Jaspars, V. M. J.: Crown-gall van tabak. Biochemisch onderzoek van weefselcultures op glucose- en zetmeelmedia. — Thesis. Leyden . 1963. 24 Jaspars, V. & Veldstra, H.: An α-amylase from tobacco crown-gall tissue cultures. II Measurements of the activity in media and tissues. Physiol. Plant. 18: 626–634. 1965. 25 Johnson, M. J.: A rapid micromethod for estimation of non-volatile organic matter. J. Biol. Chem. 181: 707–711. 1949. 26 Kaper, J. M. & Veldstra, H.: On the metabolism of tryptophan by Agrobacterium tumefaciens. Biochim. Biophys. Acta 30: 401–420. 1958. 27 Karstens, W. K. H. & Meester-Manger, Cats, V. de: The cultivation of plant tissues in vitro with starch as a source of carbon. Acta Bot. Neerl. 9: 263–274. 1960. 28 van Klinkenberg, G. A.: Over de scheiding en de werking der beide moutamylasen. — Thesis. Utrecht . 1931. 29 Krossing, G.: Versuche zur Lokalisation einiger Fermente in den verschiedenen Zell-bestandteilen der Spinatblätter. Biochem. Z. 305: 359–373. 1940. 30 Linderstrøm-Lang, K. & Lanz, H.: Studies on enzymatic histochemistry. XXIX. Dilato-metric micro-estimation of peptidase activity. Compt. Rend. Lab. Carlsberg. Sér. Chim. 21: 315–338. 1938. 31 Loyter, A. & Sehramm, M.: The glyeogen-amylase Complex as a means of obtaining highly purified α-amylases. Biochim. Biophys. Acta 65: 200–206. 1962. 32 Markert, C. L.: Lactate dehydrogenase isozymes. Dissociation and recombination of subunits. Science 140: 1329–1331. 1963. 33 Meeuse, B. J. D.: Oriënterende onderzoekingen over de vorming van rietsuiker uit zetmeel in planten bij lage temperatuur. — Thesis. Delft . 1943. 34 Meyer, K. H., Fischer, E. H. & Piquet, A.: Sur les enzymes amylolytiques. XVI. Purification et cristallization de la α-amylase de malt. Helv. Chim. Acta 34: 316–324. 1951. 35 Morel, G.: Recherehes sur la culture associée de parasites obligatoires et de tissus végétaux. Ann. Epiphyt. N. S. 14: 123–234. 1948. 36 Riker, A. J. & Hildebrandt, A. C.: Plant tissue cultures open a botanical frontier. Ann. Rev. Microbiol. 12: 469–490. 1958. 37 Schwartz, D.: Genetic studies on mutant enzymes in maize: synthesis of hybrid enzymes by heterozygotes. Proc. Natl. Acad. Sci. (U.S.) 46: 1210–1215. 1960. 38 Schwimmer, S. & Balls, A. K.: Isolation and properties of crystalline α-amylase from germinated barley. J. Biol. Chem. 179: 1063–1074. 1949. 39 Sjöberg, K.: Beiträge zur Kenntnis der Amylase in Pflanzen. I. Über die Bildung und das Verhalten der Amylase in lebenden Pflanzen. Biochem. Z. 133: 218–293. 1922. 40 Sjöberg, K. Beiträge zur Kenntnis der Amylase in Pflanzen. II. Die Temperaturempfindlichkeit der Amylase von Phaseolus vulgaris. Ibid. 133: 294–330. 1922. 41 Staples, R. C. & Stahmann, M. A.: Changes in proteins and several enzymes in susceptible bean leaves alter infection by the bean rust fungus. Phytopathology 54: 760–764. 1964. 42 Starkweather, W. H. & Shoch, H. K.: Some observations on the lactate dehydrogenase of human neoplastic tissue. Biochim, Biophys. Acta 62: 440–442. 1962. 43 Swanson, M. A.: Studies on the structure of polysaccharides. II. Degradation of polysaceharides by enzymes. J. Biol. Chem. 172: 805–814. 1948. 44 Swanson, M. A. Studies on the structure of polysaceharides. IV. Relation of the iodine colour to the structure. Ibid. 172: 825–837, 1948. 45 Vallee, B. L., Stein, E. A., Sumerwell, W. N. & Fischer, E. H.: Metal content of α-amylase. of various origins. J. Biol. Chem. 234: 2901–2905. 1959. 46 Venter, J.: Die Periodizität der Variierung in Amylaseaktivität. Z. Bot. 44: 59–76. 1956. 47 Wieland, T. & Pfleiderer, G.: Differente und multiple Formen von Enzymen. Angew. Chem. 74: 261–270. 1962. 48 Wieme, R. J.: An improved technique of agar-gel electrophoresis on microscope slides. Clin. Chim. Acta 4: 317–321. 1959. 49 Wilson, A. C., Cahn, R. D. & Kaplan, N. O.: Functions of the two forms of lactic debydrogenase in the breast muscle of birds. Nature 197: 331–334. 1963. 50 Wijsiuan, H. P.: De diastase, beschouwd als een mengsel van maltase en dextrinase. — Thesis. Amsterdam . 1889. 51 Yamamoto, T.: Studies on the bacterial α-amylase, especially in regard to the role of calcium contained. Bull. Ager. Chem. Soc. Japan 20: 188–196. 1956. Citing Literature Volume18, Issue3July 1965Pages 604-625 ReferencesRelatedInformation" @default.
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