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Toshiaki Yaguchi

Researcher at University of Tokyo

Publications -  7
Citations -  139

Toshiaki Yaguchi is an academic researcher from University of Tokyo. The author has contributed to research in topics: RuBisCO & Ribulose. The author has an hindex of 6, co-authored 7 publications receiving 134 citations.

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Phylogenetic position of an obligately chemoautotrophic, marine hydrogen-oxidizing bacterium, Hydrogenovibrio marinus, on the basis of 16S rRNA gene sequences and two form I RuBisCO gene sequences

TL;DR: Two form ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) genes from the obligately autotrophic, marine hydrogen oxidizer Hydrogenovibrio marinus were sequenced as mentioned in this paper.
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Cloning and Sequence of the L2 Form of RubisCO from a Marine Obligately Autotrophic Hydrogen-oxidizing Bacterium, Hydrogenovibrio marinus Strain MH-110

TL;DR: The deduced amino acid sequence had high homology with those of the L2-form RubisCO of Rhodospirillum rubrum and the L4-formrubulose-1,5-bisphosphate carboxylase/oxygenase from Rhodobacter sphaeroides, but low similarity to other L8S8 form Rubis COs.
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Different properties of gene products of three sets ribulose 1,5-bisphosphate carboxylase/oxygenase from a marine obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110

TL;DR: Investigation of three sets of genes for ribulose 1,5-bisphosphate carboxylase/oxygenase in Hydrogenovibrio marinus strain MH-110 revealed that the specific activity of CbbM was very low and CBBM was inactivated easily during the process of purification, and the antibody to neither form of RubisCO demonstrated cross-reactivity for the other form.
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Purification of form L2 RubisCO from a marine obligately autotrophic hydrogen-oxidizing bacterium, Hydrogenovibrio marinus strain MH-110.

TL;DR: The N-terminal amino acid sequence determination of the purified enzyme showed high homology with those of the L2-form RubisCO of Rhodospirillum rubrum and the Lx-formRubisCO from Rhodobacter sphaeroides.
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Purification of RuBisCO from the thermophilic cyanobacterium Synechococcus sp. strain a-1

TL;DR: Ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO), the key enzyme of the Calvin Benson cycle, has been purified from a thermophilic cyanobacterium, Synechococcus sp.