Starch-accumulating Sweet Potato Callus Tissue Devoid of β-Amylase but with Two Starch Phosphorylase Isozymes

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概要

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• By controlling the concentrations of kinetin, auxin, and sucrose in the Murashige-Skoog medium, starch contents in callus culture induced from sweet potato tissues could be manipulated. Activity staining and Western analysis on PAGE plates and activity assays made on starch phosphorylase in the presence and absence of mercuric ions showed that β-amylase is absent in callus cultures regardless of whether their starch content is high or low. This would imply that β-amylase induction in sweet potato calli is not linked to the metabolic control through which the expression of storage function is associated, as proposed by Nakamura et al. [Plant Physiol., 96,902 (1991)] for sweet potato leaf-petiole cuttings. Analyses of starch phosphorylase in crude extracts suggested the presence of a new starch phosphorylase in tuberous root and callus tissue. This phosphorylase is immunologically different from the tuberous root and leaf enzymes that we studied previously.

• 社団法人日本農芸化学会の論文
• 1993-08-23

著者

• Su J‐c

  National Taiwan Univ. Taipei Twn

• Su Jong-ching

  Biochemistry Laboratory Department Of Agricultural Chemistry National Taiwan University:institute Of

• Lee P‐d

  Department Of Agricultural Chemistry National Taiwan University

• Wang Heng-long

  Biochemistry Laboratory Department Of Agricultural Chemistry National Taiwan University:institute Of

• Lee Ping-Du

  Biochemistry Laboratory, Department of Agricultural Chemistry, National Taiwan University

• Juang Rong-Huary

  Biochemistry Laboratory, Department of Agricultural Chemistry, National Taiwan University

• Juang R‐h

  Biochemistry Laboratory Department Of Agricultural Chemistry National Taiwan University

関連論文

• Starch-accumulating Sweet Potato Callus Tissue Devoid of β-Amylase but with Two Starch Phosphorylase Isozymes
• Differentially and Developmentally Regulated Expression of Three Rice Sucrose Synthase Genes
• Complete Structures of Three Rice Sucrose Synthase Isogenes and Differential Regulation of Their Expressions

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