Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Masami Sugiyama"'
Autor:
Hiroshi Hashimoto, Takako Kamo, Masami Sugiyama, Naoki Hosomi, Haruo Suzuki, Yasuko Kawamura-Konishi, Rumie Sasaki, Masaaki Yamazaki, Hiroyuki Tashiro
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. :99-109
Five catalytic and nine non-catalytic antibodies for insertion of a metal ion into porphyrin were generated by immunization with N-methyl mesoporphyrin (N-MMP) as hapten, which was designed to mimic the distortion of porphyrin toward a transition-sta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b6652df64b023d7065f2ae672c4db0d5
https://doi.org/10.1016/s1381-1177(03)00134-6
https://doi.org/10.1016/s1381-1177(03)00134-6
Colorimetrical rate assay for urinary dipeptidyl peptidase IV (DPPIV) activity using a new substrate
Publikováno v:
Journal of clinical laboratory analysis. 9(2)
We synthesized a new substrate glycyl-L-proline 3,5-dibromo-4-hydroxyanilide (Gly-Pro-DBAP), for dipeptidyl peptidase IV (DPPIV). Its hydrolysis by DPPIV resulted in the formation of a chromophore, 2,6-dibromophenol-indo-p-xylenol, and its maximal ab
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c3f2cef64b467252745a11b6cade25a8
https://pubmed.ncbi.nlm.nih.gov/7714663
https://pubmed.ncbi.nlm.nih.gov/7714663
Publikováno v:
The proceedings of the JSME annual meeting. :223-224
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc82812f1f53bc9386ef6ab6836bb9b0
https://doi.org/10.1299/jsmemecjo.2002.5.0_223
https://doi.org/10.1299/jsmemecjo.2002.5.0_223
Autor:
Masami Sugiyama
Publikováno v:
The Journal of Japan Atherosclerosis Society. 7:631-634
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::569ff439b61509af17176160db310200
https://doi.org/10.5551/jat1973.7.4_631
https://doi.org/10.5551/jat1973.7.4_631
Publikováno v:
Journal of biochemistry. 94(1)
A simple and reproducible method for the determination of serum pseudo-cholinesterase activity was developed by making use of a stable substrate, p-hydroxybenzoylcholine, with p-hydroxybenzoate hydroxylase as a linked enzyme. The method is based on s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cfe0e862b321c3fbf2c63b17835601eb
https://pubmed.ncbi.nlm.nih.gov/6619102
https://pubmed.ncbi.nlm.nih.gov/6619102