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Delineation of the structural and functional role of Arg111 in GSTU4-4 from Glycine max by chemical modification and site-directed mutagenesis.

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The structural and functional role of Arg111 in GSTU4-4 from Glycine max (GmGSTU4-4) was studied by chemical modification followed by site-directed mutagenesis. The arginine-specific reagent 2,3-butanedione (BTD) inactivates the enzyme in borate buffer at pH8.0, with pseudo-first-order saturation

Volatile flavor components in red fermented soybean (Glycine max) curds.

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Red fermented soybean (Glycine max) curds (FSC) were extracted with a simultaneous steam distillation and extraction (SDE) apparatus and analyzed by gas chromatography-mass spectrometry (GC-MS) and further evaluated by gas chromatography-mass spectrometry-flame ionization detector-olfactometry

Inositol-1 (or 4)-monophosphatase from Glycine max embryo axes is a phosphatase with broad substrate specificity that includes phytate dephosphorylation.

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A phosphate-hydrolyzing activity from Glycine max embryo axes was purified by a series of chromatographic steps and electroelution from activity gels, and demonstrated to be an inositol-1 (or 4)-monophosphatase by partial internal amino acid sequence. This enzyme hydrolyzed ATP, sodium pyrophosphate

Stop-and-go movements of plant Golgi stacks are mediated by the acto-myosin system.

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The Golgi apparatus in plant cells consists of a large number of independent Golgi stack/trans-Golgi network/Golgi matrix units that appear to be randomly distributed throughout the cytoplasm. To study the dynamic behavior of these Golgi units in living plant cells, we have cloned a cDNA from

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Herbal & Natural Medicine

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