Intraspecific variability of the tandem repeats in Nicotiana putrescine N-methyltransferases

Intraspecific variability of the tandem repeats in Nicotiana putrescine N-methyltransferases Plant Molecular Biology 38: 915, 1998. © 1998 Kluwer Academic Publishers. Printed in the Netherlands. Erratum Intraspecific variability of the tandem repeats in Nicotiana putrescine N-methyltransferases Takashi Hashimoto , Tsubasa Shoji, Taku Mihara, Hideo Oguri, Katsutomo Tamaki, Ken-ichi Suzuki and Yasuyuki Yamada Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma, Nara 630-01, Japan ( author for correspondence) Table 1 was inadvertently left out in Volume 37, pp. 27–37. In the third line of the legend to Figure 5 the word ‘dome’ should read ‘some’. Table 1. Kinetic properties of recombinant PMTs (mM) recombinant kcat (s ) protein putrescine S-adenosylmethionine PMT 4:91 0:95 1:18 0:34 0:60 0:05 PMT 3:92 0:70 0:76 0:10 0:59 0:06 Enzyme activities were measured for more than six concentrations each of pu- trescine and S-adenosylmethionine. The catalytic constants (k ) were derived cat from the V values for putrescine. The full-length PMT and the truncated max PMT (PMT) without the N-terminal 81 amino acid residues were both ex- pressed in E. coli as fusion proteins to the histidine-tagged metal-binding domain. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Intraspecific variability of the tandem repeats in Nicotiana putrescine N-methyltransferases

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Publisher
Kluwer Academic Publishers
Copyright
Copyright © 1998 by Kluwer Academic Publishers
Subject
Life Sciences; Biochemistry, general; Plant Sciences; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1023/A:1006035406981
Publisher site
See Article on Publisher Site

Abstract

Plant Molecular Biology 38: 915, 1998. © 1998 Kluwer Academic Publishers. Printed in the Netherlands. Erratum Intraspecific variability of the tandem repeats in Nicotiana putrescine N-methyltransferases Takashi Hashimoto , Tsubasa Shoji, Taku Mihara, Hideo Oguri, Katsutomo Tamaki, Ken-ichi Suzuki and Yasuyuki Yamada Graduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma, Nara 630-01, Japan ( author for correspondence) Table 1 was inadvertently left out in Volume 37, pp. 27–37. In the third line of the legend to Figure 5 the word ‘dome’ should read ‘some’. Table 1. Kinetic properties of recombinant PMTs (mM) recombinant kcat (s ) protein putrescine S-adenosylmethionine PMT 4:91 0:95 1:18 0:34 0:60 0:05 PMT 3:92 0:70 0:76 0:10 0:59 0:06 Enzyme activities were measured for more than six concentrations each of pu- trescine and S-adenosylmethionine. The catalytic constants (k ) were derived cat from the V values for putrescine. The full-length PMT and the truncated max PMT (PMT) without the N-terminal 81 amino acid residues were both ex- pressed in E. coli as fusion proteins to the histidine-tagged metal-binding domain.

Journal

Plant Molecular BiologySpringer Journals

Published: Oct 6, 2004

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