TY - JOUR
T1 - Isolation and properties of an S-adenosyl-L-methionine binding protein from the green alga, Chlamydomonas reinhardi
AU - Nakano, Y.
AU - Koizumi, N.
AU - Kusano, T.
AU - Sano, H.
N1 - Funding Information:
Acknowledgements. This work was partly supported by a grant from CREST, Japan Science and Technology Corporation.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2000
Y1 - 2000
N2 - A protein that binds S-adenosyl-L-methionine (AdoMet) was isolated by successive chromatography from vegetative cells of Chlamydomonas reinhardi. The relative molecular masses of native and denatured proteins were calculated to be 15 kDa and 16 kDa, respectively. The reaction was specific to AdoMet and reversible as shown by competition experiments. The optimal pH for binding ranged between 7.5 and 9.0, and the apparent Ka for AdoMet was 1.0 μmol/L. Results suggested that the protein may function as the carrier to stabilize AdoMet, which is otherwise labile in the cellular environment.
AB - A protein that binds S-adenosyl-L-methionine (AdoMet) was isolated by successive chromatography from vegetative cells of Chlamydomonas reinhardi. The relative molecular masses of native and denatured proteins were calculated to be 15 kDa and 16 kDa, respectively. The reaction was specific to AdoMet and reversible as shown by competition experiments. The optimal pH for binding ranged between 7.5 and 9.0, and the apparent Ka for AdoMet was 1.0 μmol/L. Results suggested that the protein may function as the carrier to stabilize AdoMet, which is otherwise labile in the cellular environment.
KW - Chlamydomonas reinhardi
KW - S-adenosyl-L-methionine
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U2 - 10.1016/S0176-1617(00)80015-2
DO - 10.1016/S0176-1617(00)80015-2
M3 - Article
AN - SCOPUS:0034485246
VL - 157
SP - 707
EP - 711
JO - Journal of Plant Physiology
JF - Journal of Plant Physiology
SN - 0176-1617
IS - 6
ER -