Takashi Akazawa

ORCID: 0009-0001-5570-7199
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Research Areas
  • Photosynthetic Processes and Mechanisms
  • Enzyme Production and Characterization
  • Food composition and properties
  • Algal biology and biofuel production
  • Microbial Metabolites in Food Biotechnology
  • Hemoglobin structure and function
  • Phytase and its Applications
  • Porphyrin Metabolism and Disorders
  • Plant nutrient uptake and metabolism
  • Biofuel production and bioconversion
  • Metal-Catalyzed Oxygenation Mechanisms
  • Mitochondrial Function and Pathology
  • Biochemical and biochemical processes
  • Biotin and Related Studies
  • Polysaccharides and Plant Cell Walls
  • 3D IC and TSV technologies
  • Lipid metabolism and biosynthesis
  • Amino Acid Enzymes and Metabolism
  • Biocrusts and Microbial Ecology
  • Plant biochemistry and biosynthesis
  • Plant tissue culture and regeneration
  • Cassava research and cyanide
  • Biochemical Acid Research Studies
  • Microbial bioremediation and biosurfactants
  • GABA and Rice Research

Niigata University
2024

Miyagi University
2024

Renesas Electronics (Japan)
2005-2009

Hitachi (Japan)
2008

Renesas Electronics (United States)
2006

Agrobiotechnology Institute
2000

Universidad Publica de Navarra
2000

Nagoya University
1986-1999

Hanazono University
1991

Fundación Instituto Leloir
1991

Enzymes of sucrose degradation and glycolysis in cultured sycamore (Acer pseudoplatanus L.) cells were assayed characterized crude extracts after partial purification, an attempt to identify pathways for catabolism. Desalted cell contained similar activities (20-40 nanomoles per milligram protein minute) synthase, neutral invertase, glucokinase, fructokinase, phosphofructokinase, UDPglucose pyrophosphorylase (assayed with 2 micromolar pyrophosphate (PPi). PPi-linked phosphofructokinase...

10.1104/pp.81.4.1008 article EN PLANT PHYSIOLOGY 1986-08-01

The time sequence analysis of the starch digestion pattern thin sectioned germinating rice (Oryza sativa L.) seed specimens using film method showed that at initial stage amylase activity was almost exclusively localized in epithelium septum between scutellum and endosperm. Starch breakdown endosperm tissues began afterward; aleurone layers detectable only after 2 days. Polyacrylamide gel electrofocusing (pH 4 to 6) revealed nearly same zymogram patterns extracts, although additional bands...

10.1104/pp.63.2.336 article EN PLANT PHYSIOLOGY 1979-02-01

The presence of betaine, a quaternary ammonium compound, at concentration (0.5 molar) reported to accumulate inside Aphanothece halophytica in response increasing external salinity, slightly promoted ribulose-1,5-bisphosphate (RuBP) carboxylase activity. KCl 0.25 molar inhibited RuBP about 55%. Betaine relieved the inhibition by m and original uninhibited activity was restored 1 betaine. Other osmoregulatory solutes such as sucrose glycerol also reduced inhibition, though lesser extent than...

10.1104/pp.81.4.1044 article EN PLANT PHYSIOLOGY 1986-08-01

In a close parallel to the developmental pattern of alpha-amylase activity, rapid increase maltase activity occurred in endosperm tissue germinating rice seeds after about 4 days seed imbibition. The overall 2 hydrolytic enzyme activities strongly suggest that amylolytic breakdown is major metabolic route starch utilization seeds. Results chemical analyses sugar constituents as well measurements sucrose synthetase show scutellum site synthesis It thus supported glucose derived from reserve...

10.1104/pp.44.5.765 article EN PLANT PHYSIOLOGY 1969-05-01

10.1016/0003-9861(64)90274-7 article EN Archives of Biochemistry and Biophysics 1964-07-01

10.1016/0003-9861(68)90465-7 article EN Archives of Biochemistry and Biophysics 1968-09-01

10.1016/0006-291x(65)90716-3 article EN Biochemical and Biophysical Research Communications 1965-02-01

The functional transition of glyoxysomes to leaf peroxisomes occurs during greening germinating pumpkin cotyledons (Cucurbita sp. Amakuri Nankin). immunocytochemical protein A-gold method was employed in the analysis using glyoxysomal specific citrate synthase immunoglobulin G and peroxisomal glycolate oxidase G. labeling density decreased microbodies greening, whereas that dramatically increased. Double experiments different sizes particles show both enzymes coexist microbody transitional...

10.1104/pp.81.1.313 article EN PLANT PHYSIOLOGY 1986-05-01

Starch biosynthesis has been studied by using amyloplasts isolated from cultured cells of sycamore trees (Acer pseudoplatanus L.). Highly purified intact amyloplasts, free mitochondria and starch granules derived broken were a Percoll step gradient. Subsequently, the double silicone oil layer centrifugation technique was used to study adenylate transport in amyloplasts. An adenylate-specific carrier found be active uptake ATP, ADP, AMP, most importantly, ADPglucose (ADP-Glc). Kinetic...

10.1073/pnas.88.13.5769 article EN Proceedings of the National Academy of Sciences 1991-07-01

The initial formation site of hydrolases in germinating cereal seeds and their subsequent release were examined using the substrate-film technique. Early germination seeds, e.g., barley, wheat, rye, oat maize, α-amylase invariably appeared region epithelial cells scutellum, whereas it later gradually diffused into entire endosperm tissues. proteinase RNA-ase barley was also confirmed to be epithelium. We conclude that epithelium has a more important role enzymic breakdown reserve substances...

10.1093/oxfordjournals.pcp.a075983 article EN Plant and Cell Physiology 1980-02-01

The methylation of nuclear and chloroplast DNAs has been examined in relation to the known differential expression C4 photosynthesis genes bundle sheath mesophyll cells etiolated, greening, fully green maize leaves. We have focused our research on phosphoenolpyruvate carboxylase, pyruvate, orthophosphate dikinase, small subunit ribulose-1,5-bisphosphate carboxylase/oxygenase (RBUp2Case) which are coded by genes, large RBUp2Case is a plastid gene. Reversed-phase high performance liquid...

10.1016/s0021-9258(18)83175-1 article EN cc-by Journal of Biological Chemistry 1989-05-01

The formation of amylase isozymes in germinating rice (Oryza sativa) seeds was studied by isoelectric focusing on polyacrylamide gel disc electrophoresis. Time sequence comparisons the zymogram were made between extracts from gibberellic acid-treated embryoless and embryo-attached half-endosperm seeds. In both cases, 4 major 9 to 10 minor isozyme bands detectable at maximal stage enzyme induction. However, half-seeds, started diminish after 5th day incubation, agreement with results time...

10.1104/pp.46.5.650 article EN PLANT PHYSIOLOGY 1970-11-01

An open reading frame, rbcR, was identified 226 bp upstream of rbcAB, i.e., the ribulose 1,5-bisphosphate carboxylase genes expressed in phototrophic purple bacterium Chromatium vinosum. Several features reveal that rbcR encodes a member LysR family transcriptional regulators, which an anomalous content lysine and arginine residues (Lys/Arg anomaly) found. The expression Escherichia coli as protein fused to N-terminal region beta-galactosidase led reduced rbcAB. Thus, is likely encode...

10.1128/jb.173.16.5224-5229.1991 article EN Journal of Bacteriology 1991-08-01

Two sets of genes for the large and small subunits ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO) were detected in photosynthetic purple sulfur bacterium Chromatium vinosum by hybridization analysis with RuBisCO gene probes, cloned using lambda Fix vector, designated rbcL-rbcS rbcA-rbcB. rbcL rbcA encode subunits, rbcS rbcB subunits. was same as that reported previously (A. M. Viale, H. Kobayashi, T. Takabe, Akazawa, FEBS Lett. 192:283-288, 1985). A DNA fragment bearing rbcA-rbcB...

10.1128/jb.171.5.2391-2400.1989 article EN Journal of Bacteriology 1989-05-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure and function of chloroplast proteins. XXIV. Spinach leaf ribulosebisphosphate carboxylase. Carboxylase oxygenase reaction examined by immunochemical methodsMikio Nishimura Takashi AkazawaCite this: Biochemistry 1974, 13, 11, 2277–2281Publication Date (Print):May 1, 1974Publication History Published online1 May 2002Published inissue 1 1974https://pubs.acs.org/doi/10.1021/bi00708a006https://doi.org/10.1021/bi00708a006research-articleACS...

10.1021/bi00708a006 article EN Biochemistry 1974-05-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure and function of chloroplast proteins. XIV. Subunit structure spinach leaf ribulose 1,5-diphosphate carboxylaseTakashi Akazawa Tatsuo SugiyamaCite this: Biochemistry 1970, 9, 23, 4499–4504Publication Date (Print):November 1, 1970Publication History Published online1 May 2002Published inissue 1 November 1970https://pubs.acs.org/doi/10.1021/bi00825a006https://doi.org/10.1021/bi00825a006research-articleACS PublicationsRequest reuse...

10.1021/bi00825a006 article EN Biochemistry 1970-11-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure and function of chloroplast proteins. XVI. Ribulose 1,5-diphosphate carboxylase from Chromatium strain DT. Akazawa, H. Kondo, Tetsuko Shimazue, M. Nishimura, T. SugiyamaCite this: Biochemistry 1972, 11, 7, 1298–1303Publication Date (Print):March 1, 1972Publication History Published online1 May 2002Published inissue 1 March 1972https://pubs.acs.org/doi/10.1021/bi00757a028https://doi.org/10.1021/bi00757a028research-articleACS...

10.1021/bi00757a028 article EN Biochemistry 1972-03-01

It has long been believed that phosphorylase is involved in the synthesis of starch, which constitutes 70 to 80% mature rice grain. Aimi and his associates (1, 2, 3) found during ripening process a parallel relationship exists between starch activity grains. But we can not exclude possible existence mechanisms other than reaction for formation. The high ratio inorganic phosphate sugar plants, unfavorable formation 10, 31), raises doubts about role polysaccharide synthesis. An important...

10.1104/pp.39.3.371 article EN PLANT PHYSIOLOGY 1964-05-01

10.1016/0006-291x(64)90203-7 article EN Biochemical and Biophysical Research Communications 1964-05-01

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSubunit structure of ribulose 1,5-diphosphate carboxylase from Chlorella ellipsoideaT. Sugiyama, Tomoko Ito, and T. AkazawaCite this: Biochemistry 1971, 10, 18, 3406–3411Publication Date (Print):August 1, 1971Publication History Published online1 May 2002Published inissue 1 August 1971https://pubs.acs.org/doi/10.1021/bi00794a014https://doi.org/10.1021/bi00794a014research-articleACS PublicationsRequest reuse permissionsArticle...

10.1021/bi00794a014 article EN Biochemistry 1971-08-01
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