Title: Purification and properties of dihydroxyacetone synthase from the methylotrophic yeast <i>Candida boidinii</i>
Abstract: FEBS LettersVolume 132, Issue 2 p. 324-328 Full-length articleFree Access Purification and properties of dihydroxyacetone synthase from the methylotrophic yeast Candida boidinii L.V. Bystrykh, L.V. Bystrykh Institute of Biochemistry and Physiology of Microorganisms, USSR Academy of Sciences, Poustchino, Moscow region, 142292, USSRSearch for more papers by this authorA.P. Sokolov, A.P. Sokolov Institute of Biochemistry and Physiology of Microorganisms, USSR Academy of Sciences, Poustchino, Moscow region, 142292, USSRSearch for more papers by this authorY.A. Trotsenko, Y.A. Trotsenko Institute of Biochemistry and Physiology of Microorganisms, USSR Academy of Sciences, Poustchino, Moscow region, 142292, USSRSearch for more papers by this author L.V. Bystrykh, L.V. Bystrykh Institute of Biochemistry and Physiology of Microorganisms, USSR Academy of Sciences, Poustchino, Moscow region, 142292, USSRSearch for more papers by this authorA.P. Sokolov, A.P. Sokolov Institute of Biochemistry and Physiology of Microorganisms, USSR Academy of Sciences, Poustchino, Moscow region, 142292, USSRSearch for more papers by this authorY.A. Trotsenko, Y.A. Trotsenko Institute of Biochemistry and Physiology of Microorganisms, USSR Academy of Sciences, Poustchino, Moscow region, 142292, USSRSearch for more papers by this author First published: September 28, 1981 https://doi.org/10.1016/0014-5793(81)81189-1Citations: 31AboutPDF 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 References 1 J.P. Van Dijken, W. Harder, A.J. Beardsmore, J.R. Quayle, FEMS Microbiol. Lett., 4, (1978), 97– 102. 2 W. Babel, N. Loffhagen, Z. Allg. Mikrobiol., 19, (1979), 299– 302. 3 N. Kato, T. Nishizawa, C. Sakazawa, Y. Tani, H. Yamada, Agr. Biol. Chem., 43, (1979), 2013– 2015. 4 S.V. Bykovskaya, Yu.A. Trotsenko, Mikrobiologiya, 49, (1980), 695– 701. 5 M.L. O'Connor, J.R. Quayle, J. Gen. Microbiol., 120, (1980), 219– 225. 6 L.V. Bystrykh, A.P. Sokolov, Yu.A. Trotsenko, Dokl. Acad. Nauk SSSR, 258, (1981), 499– 502. 7 A.G. Datta, E. Racker, J. Biol. Chem., 236, (1961), 617– 623. 8 M.M. Bradford, Anal. Biochem., 72, (1976), 248– 254. 9 Polyacrylamide Gel Electrophoresis (1980), Pharmacia Fine Chemicals Uppsala 28– 35. Laboratory techniques 10 G.A. Kochetov, P.P. Philippov, R.A. Usmanov, Biokhimiya, 34, (1969), 810– 812. 11 R.L. Aikth, G.E. Foerster, Methods Enzymol., 18, (1970), 81– 86. 12 J. Saitou, T. Ozawa, I. Tomita, FEBS Lett., 40, (1974), 114– 118. 13 H. Klein, K. Brand, Hoppe-Seyler's Z. Physiol. Chem., 358, (1977), 1325– 1337. 14 F. Dickens, D.H. Williamson, Nature, 181, (1958), 1790– 15 J.J. Villafranca, B. Axelrod, J. Biol. Chem., 246, (1971), 3126– 3131. 16 T. Wood, A. Gascon, Arch. Biochem. Biophys., 203, (1980), 727– 733. 17 S.W. Cavalieri, K.E. Neet, H.Z. Sable, Arch. Biochem. Biophys., 171, (1975), 527– 532. 18 R. Bieber, G. Trumpler, Helv. Chim. Acta, 30, (1947), 1860– 1865. 19 P. Strittmatter, E.G. Ball, J. Biol. Chem., 213, (1955), 445– 461. Citing Literature Volume132, Issue2September 28, 1981Pages 324-328 ReferencesRelatedInformation