Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Chikafusa Fukazawa"'
Publikováno v:
Nippon Shokuhin Kagaku Kogaku Kaishi. 57:150-156
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b23b97798e861dab4a2b1512e8738ac2
https://doi.org/10.3136/nskkk.57.150
https://doi.org/10.3136/nskkk.57.150
Publikováno v:
Biochemistry. 46:792-798
Beta-amylase (EC 3.2.1.2) is starch-hydrolyzing exo-type enzyme that can catalyze the successive liberation of beta-maltose from the nonreducing ends of alpha-1,4-linked glucopyranosyl polymers. There is a well-known phenomenon called multiple or rep
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b9a063bf35d2cba452b76448063f283f
https://doi.org/10.1021/bi061605w
https://doi.org/10.1021/bi061605w
Publikováno v:
European Journal of Biochemistry. 267:2649-2657
A soybean protein was purified from mature dry seeds. Amino-acid sequencing of the nine internal peptides derived from this N-terminally blocked protein showed that it has a significant similarity to the soluble epoxide hydrolases known to date. A de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::501f45759c4a98859f9ea4841504c5a0
https://doi.org/10.1046/j.1432-1327.2000.01276.x
https://doi.org/10.1046/j.1432-1327.2000.01276.x
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 63:726-730
Authentic soybean β-amylase preparation, purified to homogeneity as judged by SDS-PAGE by using an affinity purification step, was composed of four pI-differing isoforms. By chromatofocusing, these isoforms were separated into three fractions, desig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e78ba42b2f187a9452fb03ae463028e1
https://doi.org/10.1271/bbb.63.726
https://doi.org/10.1271/bbb.63.726
Autor:
Chikafusa Fukazawa, Van Hai Nong, Masaomi Arahira, Deyu Zhang, Akira Watanabe, Nana Asare Yeboah, Kazunari Kadokura
Publikováno v:
Plant Molecular Biology. 36:407-415
A soybean chitinase which has an apparent molecular mass of 28 kDa by SDS-PAGE, and has chitinase specific activity of 133 units per mg protein at pH 5.2 and an apparent pI of 5.7, was purified from mature dry seeds. Based upon the selected part (the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::388681a1f9c5d5a88c3a17e06e5eacf5
https://doi.org/10.1023/a:1005921104288
https://doi.org/10.1023/a:1005921104288
Autor:
Atsushi Totsuka, Chikafusa Fukazawa
Publikováno v:
European Journal of Biochemistry. 240:655-659
Soybean beta-amylase, comprising a (beta/alpha)8-barrel core with a mobile loop, similar to that of triose phosphate isomerase, was mutated by site-directed mutagenesis at residues Glu380 and Leu383. X-ray crystallographic findings suggest that Glu38
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a906f676a975b5a37c7c005e8ea0de9d
https://doi.org/10.1111/j.1432-1033.1996.0655h.x
https://doi.org/10.1111/j.1432-1033.1996.0655h.x
Autor:
Chan-Shick Kim, Hiroya Kadokawa, Chikafusa Fukazawa, Hai Van Nong, Atsushi Totsuka, Yoshifumi Itoh
Publikováno v:
European Journal of Biochemistry. 221:649-654
To determine which amino acid residues are essential for the catalytic activity of soybean P-amylase, deoxyoligonucleotide site-directed mutagenesis was employed against aspartyl, glutamyl, and cysteinyl residues located in highly conserved regions f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::48489a35878e8a24007896c3d22a4c44
https://doi.org/10.1111/j.1432-1033.1994.tb18777.x
https://doi.org/10.1111/j.1432-1033.1994.tb18777.x
Publikováno v:
Plant and Soil. :211-214
Glutelin accumulation in the apical spikelet of the top primary branch (superior spikelet) and the second spikelet of the lowest secondary branch (inferior spikelet) of the ear of the rice plant (Oryza sativa L.) was characterized during grain fillin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ab519fe8479943450322375055b0a279
https://doi.org/10.1007/bf00025021
https://doi.org/10.1007/bf00025021
Autor:
Kiyoshi Sugawara, Naoko Minami, Yoshimi Kobayashi, Chikafusa Fukazawa, Hidenari Takahara, Tomoji Arai, Hiroaki Tsujimoto, Mamoru Tsuchida
Publikováno v:
European Journal of Biochemistry. 215:677-685
Peptidylarginine deiminase is a protein-modulating enzyme which converts the arginine residues in proteins to citrulline residues. This study describes the complete primary structure of mouse peptidylarginine deiminase, which was deduced from nucleot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89048fa3c0a61296007c367bb19dc28e
https://doi.org/10.1111/j.1432-1033.1993.tb18079.x
https://doi.org/10.1111/j.1432-1033.1993.tb18079.x
Publikováno v:
European Journal of Biochemistry. 215:123-132
During seed embryogenesis, glycinin, the 11-S seed storage protein found in soybeans, undergoes post-translational proteolytic processing, in which a proprotein molecule is cleaved into an acidic and a basic subunit by a one-point cleavage that occur
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e28927bc7e22b05fa8316800b45e0b2e
https://doi.org/10.1111/j.1432-1033.1993.tb18014.x
https://doi.org/10.1111/j.1432-1033.1993.tb18014.x