Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Yasushi Shirahase"'
Autor:
Kazu Hatanaka, Yasushi Shirahase, Toshiyuki Yoshida, Mari Kono, Naoki Toya, Shin-Ichi Sakasegawa, Kenji Konishi, Tadashi Yamamoto, Kuniyasu Ochiai, Shogo Takashiba
Publikováno v:
PLoS ONE, Vol 17, Iss 7, p e0268671 (2022)
Periodontal disease is a chronic inflammatory condition caused by periodontal pathogens in the gingival sulcus. Short-chain fatty acids (SCFAs) produced by causal bacteria are closely related to the onset and progression of periodontal disease and ha
Externí odkaz:
https://doaj.org/article/b8053b94526a451e8ad19ad0ed6a9eda
Autor:
Hiroaki Okabe, Nobuaki Kaneda, Sawao Murao, Yoshifumi Watazu, Katashi Nagamatsu, Yasushi Shirahase
Publikováno v:
Bioscience, Biotechnology, and Biochemistry. 58:745-751
A selective inactivating enzyme for the m-subunit of lactate dehydrogenase (LDH) was found in the culture filtrate of Penicillium citrinum KE-1, newly isolated from soil. The enzyme was purified from the culture filtrate by ammonium sulfate fractiona
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e96141460f7c373bfaeffd9d9d1f068
https://doi.org/10.1271/bbb.58.745
https://doi.org/10.1271/bbb.58.745
Autor:
Yasushi Shirahase, Arthur Karmen, Nobuaki Kaneda, Hiroaki Okabe, Yoshifumi Watazu, Yoshinori Uji
Publikováno v:
Journal of Clinical Laboratory Analysis. 7:81-85
We studied a new proteinase K assay method for human serum mitochondrial aspartate aminotransferase. We found that proteinase K showed no inactivation of human mitochondrial aspartate aminotransferase isoenzyme and complete inactivation of cytosolic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dabf9cf7706f950a8c6088f23af6d18a
https://doi.org/10.1002/jcla.1860070202
https://doi.org/10.1002/jcla.1860070202
Autor:
Ayumi Asaeda, Kazuaki Yamashita, Mitsuru Yanai, Yasushi Shirahase, Yasuhiro Sakai, Kazunari Kumasaka, Kouji Sakaguchi, Theo Wallimann, Uwe Schlattner, Tadashi Hoshino, Kouji Kishi
Publikováno v:
Scandinavian Journal of Clinical and Laboratory Investigation
Scandinavian Journal of Clinical and Laboratory Investigation, Taylor & Francis, 2009, pp.1-9. ⟨10.1080/00365510902981171⟩
Scandinavian Journal of Clinical and Laboratory Investigation, Taylor & Francis, 2009, pp.1-9. ⟨10.1080/00365510902981171⟩
International audience; Objective: The MB fraction of creatine kinase (CK-MB) has long been used as a cardiac marker. It is known that the CK-MB immunoinhibition method lacks selectivity and accuracy, because the appearance of macro CK type 2, corres
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e511da8788d49b0ad52454b9ac50a793
https://pubmed.ncbi.nlm.nih.gov/19484658
https://pubmed.ncbi.nlm.nih.gov/19484658
Publikováno v:
Journal of clinical laboratory analysis. 10(2)
~We have developed a new automated method for the determination of malate dehydrogenase (MDH) isoenzymes in serum employing guanidine hydrochloride. Our proposed method showed good reproducibility; within-run precision coefficient of variations (CVs)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14ba3811a2c9a63201d0e2eb4e41a06b
https://pubmed.ncbi.nlm.nih.gov/8852359
https://pubmed.ncbi.nlm.nih.gov/8852359
Autor:
Nobuaki Kaneda, Yasushi Shirahase, Hiroyuki Sugiuchi, Yoshinori Uji, Yoshifumi Watazu, Hiroaki Okabe
Publikováno v:
Clinical biochemistry. 23(2)
A new proteolytic measurement of serum mitochondrial aspartate aminotransferase was evaluated using cytosolic aspartate aminotransferase inactivating protease. Some of the proteases, such as, alpha-chymotrypsin, subtilisin and cytosolic aspartate ami
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61e9ef3e4c7ba2e778616d55148364f5
https://pubmed.ncbi.nlm.nih.gov/2197026
https://pubmed.ncbi.nlm.nih.gov/2197026
Publikováno v:
Journal of the American Chemical Society. 105:4400-4407
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::de80b8132554e8e4675aaf2ae0ed647a
https://doi.org/10.1021/ja00351a046
https://doi.org/10.1021/ja00351a046