Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Hiroo Yonezawa"'
Publikováno v:
Bioscience, biotechnology, and biochemistry. 63(8)
Fluorogenic substrates for cathepsin D; A-Tyr-Phe(NO2)-Leu-Leu (A; Ala-Arg-Pro-Lys-Pro-Leu-Leu-, Arg-Pro-Lys-Pro-Leu-Leu-, Pro-Lys-Pro-Leu-Leu-, Lys-Pro-Leu-Leu-, Pro-Leu-Leu-) and B-Phe(NO2)-Tyr-Leu-Leu (B; Arg-Pro-Lys-Pro-Leu-Leu-, Pro-Lys-Pro-Leu-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ab1638ebf739dd2a4de60a5377d02cc
https://pubmed.ncbi.nlm.nih.gov/27389509
https://pubmed.ncbi.nlm.nih.gov/27389509
Publikováno v:
International Journal of Peptide and Protein Research. 25:640-647
K-582 A, an antibiotic heptapeptide, has a sequence of H-L-Arg-L-Arg(OH)-D-Orn-L-Thr-D-Orn-L-Lys-D-Tyr-OH (Arg(OH), threo-gamma-hydroxyarginine). In order to investigate the relationship between structure and antimicrobial activity, four shortened an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2f7387211d1ed30c27644d1bbe5b8fa
https://doi.org/10.1111/j.1399-3011.1985.tb02221.x
https://doi.org/10.1111/j.1399-3011.1985.tb02221.x
Autor:
Michiko Okubo, Tetsuya Uchikoba, Michio Onjo, Hiroo Yonezawa, Shigeko Fukumoto, Kazunari Arima
Publikováno v:
Journal of Thermal Biology. 28:555-562
Freesia protease (FP)-A has been found in regular freesia corms (Kaneda et al., Biosci. Biotechnol. Biochem. 61 (1997) 1554). New corms were generated from original corms that were kept for several months at 4°C. In this study, two proteases (FP-B a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6a8da7884548fcf199a3626b245104a3
https://doi.org/10.1016/j.jtherbio.2003.07.001
https://doi.org/10.1016/j.jtherbio.2003.07.001
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 66:448-452
A protease, freesia protease (FP)-A, was purified to electrophoretic homogeneity from regular freesia (Freesia reflacta) corms in harvest time. The Mr of FP-A was estimated to be 24 k by SDS-PAGE. The optimum pH of the enzyme was 8.0 using a casein s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c1955fefa5fdfbd4ab6146bb119af94
https://doi.org/10.1271/bbb.66.448
https://doi.org/10.1271/bbb.66.448
Publikováno v:
Journal of Biochemical and Biophysical Methods. 48:303-308
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2e6c088f84b1979b237ebc8c219c0dab
https://doi.org/10.1016/s0165-022x(01)00164-6
https://doi.org/10.1016/s0165-022x(01)00164-6
Autor:
Hiroo Yonezawa, Tetsuya Uchikoba, Michio Onjyo, Kazunari Arima, Makoto Kaneda, Saburo Hosoyamada
Publikováno v:
Phytochemistry. 57:1-5
An endopeptidase from the fruits of Melothria japonica (Thunb.) Maxim. has been purified by DEAE-Sepharose chromatography and gel-filtration by a Sephacryl S-300. The enzyme has Mr of 61 kDa. The optimum pH of the enzyme was 8. The enzyme activity wa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::94af2e5acfa5a1ca33db61b4b8b9e318
https://doi.org/10.1016/s0031-9422(00)00511-2
https://doi.org/10.1016/s0031-9422(00)00511-2
Publikováno v:
Phytochemistry. 54:559-565
An endopeptidase has been purified from sprouts of bamboo (Pleioblastus hindsii Nakai) to electrophoretic homogeneity by four purification steps. Its Mr was estimated to be 82 kDa by SDS-PAGE. Enzyme activity was inhibited strongly by diisopropyl flu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::faf33c56549c0127b1fdf96aad26ee83
https://doi.org/10.1016/s0031-9422(00)00075-3
https://doi.org/10.1016/s0031-9422(00)00075-3
Publikováno v:
Phytochemistry. 54:451-454
The substrate specificity of a plant serine protease, cucumisin (EC 3.4.21.25), was studied by the use of synthetic oligopeptides and peptidyl- p NA substrates. Since P1′-Ser, Ala, and Gly substrates were hydrolyzed rapidly, cucumisin appears to pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee16595a579183599be2bc0bebd795e7
https://doi.org/10.1016/s0031-9422(00)00157-6
https://doi.org/10.1016/s0031-9422(00)00157-6
Publikováno v:
Journal of Biochemistry. 126:26-33
A cysteine protease, phytolacain R from full-growth greenish fruits of pokeweed, Phytolacca americana L, was purified to electrophoretic homogeneity by a simple purification procedure employing CM-Sepharose ion-exchange chromatography. The enzyme was
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c385179eb31048cfaa946cc4e1537160
https://doi.org/10.1093/oxfordjournals.jbchem.a022431
https://doi.org/10.1093/oxfordjournals.jbchem.a022431
Publikováno v:
Phytochemistry. 49:2215-2219
A protease has been purified from the sarcocarp of Benincasa hispida (Thunb.) Cogn. var. Ryukyu by two steps of chromatography. Its M r was estimated by SDS–PAGE to be about 67,000. The enzyme was strongly inhibited by diisopropyl fluorophosphate,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82dd10339b2973a2f2b94bbff5a16373
https://doi.org/10.1016/s0031-9422(98)00135-6
https://doi.org/10.1016/s0031-9422(98)00135-6