Zobrazeno 1 - 10
of 97
pro vyhledávání: '"Tsutomu Yasui"'
Publikováno v:
InnoSWDev@SIGSOFT FSE
In this paper, we propose a new business model for custom software development industry utilizing agile software development to embrace changes. Traditional business model usually does not work well with agile software development because it mandate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f0aecde2e7781ce45c5d590cf766318
https://doi.org/10.1145/2666581.2666584
https://doi.org/10.1145/2666581.2666584
Publikováno v:
The Journal of Biochemistry. 116:215-220
Hydrostatic pressure-induced morphological and physiochemical changes in monomeric myosin were investigated. The turbidity of a myosin solution increased after release of pressure, indicating aggregation of the molecules. Some molecules were single h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0004e3f16a42e8451c37a13c274c2fcd
https://doi.org/10.1093/oxfordjournals.jbchem.a124496
https://doi.org/10.1093/oxfordjournals.jbchem.a124496
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 57:383-389
Myosin dissolved in 0.5 M KCl at pH 6.0 was exposed to hydrostatic pressure up to 210 MPa for 30 min. Turbidity of myosin solutions did not change after application of pressure at 70 MPa, while it gradually increased with extending duration of pressu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d519dc8352fa9e9310757bb88722f46a
https://doi.org/10.1271/bbb.57.383
https://doi.org/10.1271/bbb.57.383
Publikováno v:
Journal of Food Science. 56:884-890
Heat-induced gelation was studied to examine the reason for marked differences in gel strength of myosins at 0.6M KCl and pH 5–6. When leg myosin (L-myosin) or L-myosin tail subfragment was mixed with breast myosin (B-myosin) or B-myosin tail subfr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::02c7240063670a75e72b795e60ebd6cd
https://doi.org/10.1111/j.1365-2621.1991.tb14598.x
https://doi.org/10.1111/j.1365-2621.1991.tb14598.x
Autor:
Jun-Ichiro Morita, Tsutomu Yasui
Publikováno v:
Agricultural and Biological Chemistry. 55:597-599
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b56b3e9e52ef3005270eecfb6c1b0d47
https://doi.org/10.1080/00021369.1991.10870607
https://doi.org/10.1080/00021369.1991.10870607
Autor:
Tsutomu Yasui, Jun-ichiro Morita
Publikováno v:
Agricultural and Biological Chemistry. 55:597-599
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8fe5cbc5325c22e4ff78059c58fd4d03
https://doi.org/10.1271/bbb1961.55.597
https://doi.org/10.1271/bbb1961.55.597
Autor:
Tsutomu Yasui
Publikováno v:
Hiroshima Math. J. 29, no. 3 (1999), 579-590
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d178438f6b2ca917f7e4b8de769d334d
https://doi.org/10.32917/hmj/1206124855
https://doi.org/10.32917/hmj/1206124855
Publikováno v:
Agricultural and Biological Chemistry. 48:2225-2232
Some physico-chemical and heat-induced gelling properties of myosin heavy chains (MHCs) from rabbit skeletal muscle were studied. MHCs were found to be almost devoid of ATPase activity, possibly because of the absence of myosin light chains. MHCs for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9cf2be2d32bb37d2da6fb13d3046f353
https://doi.org/10.1271/bbb1961.48.2225
https://doi.org/10.1271/bbb1961.48.2225
Publikováno v:
Agricultural and Biological Chemistry. 49:2975-2983
Some physicochemical and functional properties of cardiac myosin were studied in a model system, with particular reference to its binding ability in re-structured meat. We found that myosin solubility was strongly influenced by the pH, ionic strength
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06ef43187d2ce80d31c3360963b79c15
https://doi.org/10.1271/bbb1961.49.2975
https://doi.org/10.1271/bbb1961.49.2975
Publikováno v:
Agricultural and Biological Chemistry. 53:625-630
Myosin rod fragments were prepared from both chicken leg and breast muscles to examine the reason for differences in the heat-induced gel strengths of these myosins at high ionic strength and low pH. The heat-induced gelation of the myosin rods was s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6ca7be0eea933bcf2a6a6e5e3da6ab2
https://doi.org/10.1080/00021369.1989.10869370
https://doi.org/10.1080/00021369.1989.10869370