Tetsuya Kumamaru

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Rice storage proteins of the endosperm are localized in two types of protein bodies, PB-I and PB-II. Protein bodies were isolated by sucrose density gradient centrifugation from developing endosperm of three rice mutants, CM 21, CM 1675 and CM 1834, and characterized after pepsin-digestion treatment by protein contents determination. Mutant protein bodies(More)
Biphenyl dioxygenases (BP Dox) from different organisms, which are involved in the initial oxygenation and subsequent degradation of polychlorinated biphenyls (PCB), are similar in structure but have different functions. The large subunit of BP Dox, encoded by the bphA1 gene, is crucial for substrate selectivity. Using the process of DMA shuffling, we(More)
Rice glutelins consist of acidic (α) and basic (β) subunits which are further separated into three polypeptide components assigned as α-1, α-2, and α-3 subunit components and β-1, β-2 and β-3 subunit components. Nine rice mutant lines with a decreased amount of the glutelin α-2 subunit component (α-2L) were obtained by screening about 6,800 potential mutant(More)
Four rice (Oryza sativa L.) mutant lines lacking glutelin alpha-1 subunit were obtained by screening the progenies of fertilized egg treatment with MNU. SDS-PAGE and IEF analyses showed that the mutants without pI6.82 polypeptide in common while forming/increasing other polypeptide indicating that the mutants were controlled by structural genes. IEF(More)
The rice (Oryza sativa L.) mutant of glu4a, lacking the glutelin α-2 subunit while the α-1 subunit increased (α-1H/α-2L), was used in this study. Two-dimensional electrophoresis analysis revealed that the mutant lacked the polypeptide pI6.71/α-2 encoded by glu4 while forming a new polypeptide of pI6.50/α-1. Experiments were conducted to identify the(More)
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