Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Toshibumi, KIYOHARA"'
Publikováno v:
武庫川女子大学紀要. 自然科学編. 50:91-95
Four proteins (BCP -IA, -IB1, -IB2 and -II) having chitin-binding ability were purified from seeds of buckwheat (Fagopyrum esculentum cv Shinano No.2) by affinity chromatography, ion-ex-change chromatography, and reverse-phase HPLC. All these protein
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::229bb18b819cc0c15cb79ea5d877dd10
http://id.nii.ac.jp/1479/00000424/
http://id.nii.ac.jp/1479/00000424/
Publikováno v:
武庫川女子大学紀要. 自然科学編. 47:29-34
Tubulin, which is a main component of the cytoskeleton, plays various important roles in cellular processes such as axonal transport, ciliary and flagellar movement, cell division, and cell segregation in the form of microtubules. The aim of the pres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::c26692d484af77c099280a2888023757
http://id.nii.ac.jp/1479/00000363/
http://id.nii.ac.jp/1479/00000363/
Autor:
Erina, SAKAMOTO, Atsuko, Iemoto, Tokumitsu, Okamura, Noboru, HORIE, Masahiro, Osugi, Toshibumi, KIYOHARA
Publikováno v:
武庫川女子大学紀要. 自然科学編. 46:27-31
The low molecular weight proteins which had affinity for chitin were purified in two types of crystalline forms from buckwheat seeds and named as buckwheat chitin-binding proteins I and II, BCP I and II. respectively. To elucidate biological properti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::467787b2062a1492c732976dc7cec4fe
http://id.nii.ac.jp/1479/00000338/
http://id.nii.ac.jp/1479/00000338/
Publikováno v:
武庫川女子大学紀要. 自然科学編. 46:21-26
Two low molecular weight proteins were separately isolated in crystalline forms from buckwheat seeds by affinity chromatography on a chitin column, ion exchange chromatography on a CM-cellulose column and gel filtration through a Sephadex G-25 column
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::ffd1dc528e25b93195cb4301cd98b010
http://id.nii.ac.jp/1479/00000337/
http://id.nii.ac.jp/1479/00000337/
Publikováno v:
武庫川女子大学紀要. 自然科学編. 45:33-37
Purification of protease from culture broth of Tricholoma sp. W510 was performed by ammonium sulfate fractionation, ion exchange column chromatography, gel filtration and butyl-toyopearl chromatographey. The enzyme was purified as one band on SDS-ele
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::e5b826b35349b69fb2dc2964c1fcb1ad
http://id.nii.ac.jp/1479/00000319/
http://id.nii.ac.jp/1479/00000319/
Autor:
Reiko, HIRASAWA, Izumi, GOTO, Tokumitsu, OKAMURA, Noboru, HORIE, Toshibumi, KIYOHARA, Masahiro, OSUGI
Publikováno v:
武庫川女子大学紀要. 自然科学編. 45:21-24
Cultivation condition of production of fibrinolytic active substance derived from Basidiomycetes was investigated. Basidiomycetes used were 11 strains of commercial product and 30 strains isolated from nature. Fibrinolytic activities were found in Ta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::c3ffa5af91ebe28219367dc13fa99c40
http://id.nii.ac.jp/1479/00000316/
http://id.nii.ac.jp/1479/00000316/
Publikováno v:
武庫川女子大学紀要. 自然科学編. 45:29-32
Proteolytic activities of culture broth of basidiomycetes were determind. Basidiomycetes used were 12 strains of commercial product and 40 strains of Isolants from nature. Proteolytic activities were found in tamogitake, mushroom and Isolant W510 bel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::94859e4baa37dd58d6d178da6fe5eae9
http://id.nii.ac.jp/1479/00000318/
http://id.nii.ac.jp/1479/00000318/
Publikováno v:
武庫川女子大学紀要. 自然科学編. 45:25-27
Mycerial cultivation of Basidiomycetes of commercial products (11 strains) and Isolants (43 strains) from nature was carried out. Of Basidiomycetes tested, Tricholoma sp. W510, which was isolated from nature, showed a strong firinolytic activity in c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=jairo_______::b701af8747f9fab28b05e59232b5ce0f
http://id.nii.ac.jp/1479/00000317/
http://id.nii.ac.jp/1479/00000317/