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PLANT PHYSIOLOGY , Vol 110, Issue 4 1395-1404, Copyright © 1996 by American Society of Plant Biologists
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BIOCHEMISTRY AND ENZYMOLOGY |
Physicochemical and Serological Characterization of Rice [alpha]-Amylase Isoforms and Identification of Their Corresponding Genes
T. Mitsui, J. Yamaguchi and T. Akazawa
Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, Ikarashi, Niigata 950-21, Japan (T.M.)
We have identified, purified, and characterized 10 [alpha]-amylase isoforms
from suspension-cultured rice (Oryza sativa L.) cells having different
isoelectric point values. They had distinguishable optimum temperatures for
enzymatic activity and molecular sizes. The results of immunoblotting
indicated that polyclonal anti-A + B antibodies bound well to isoforms A,
B, Y, and Z but weakly or not at all to E, F, G, H, I, and J. However, the
anti-A + B antibodies inhibited the enzyme activities of only isoforms A
and B. Polyclonal anti-H antibodies strongly bound to isoforms F, G, H, I,
and J, whereas polyclonal anti-E antibodies preferentially recognized
isoform E. A monoclonal antibody against isoform H (H-G49) inhibited the
activities of isoforms E, G, H, I, and J, whereas it did not inhibit those
of isoforms A, B, Y, and Z. Judging from their physicochemical and
serological properties, we classified the rice [alpha]-amylase isoforms
into two major classes, class I (A, B, Y, and Z) and class II (E, F, G, H,
I, and J), and into four subgroups, group 1 (A and B), group 2 (Y and Z),
group 3 (E), and group 4 (F, G, H, I, and J). Partial amino acid sequences
for isoforms A, E, G, and H were also determined. In addition, the
recombinant [alpha]-amylases expressed by plasmid pEno/103 containing the
rice [alpha]-amylase gene RAmy1A in yeast were identified as both isoforms
A and B. These analyses indicated that isoforms A and B were encoded by the
gene RAmy1A, isoforms G and H were encoded by the gene RAmy3D, and isoform
E was encoded by RAmy3E. The results strongly suggest that some isoforms
within subgroups are formed by posttranslational modifications.
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