Zobrazeno 1 - 10 of 31 pro vyhledávání: '"Senarath B. P. Athauda"'
1
Heat stability of the in vitro inhibitory effect of spices on lipase, amylase, and glucosidase enzymes
Autor: Lalith Jayasinghe, Nimal Savitri Kumar, Ramiah Sivakanesan, Kumudu Irani Perera, Senarath B. P. Athauda, Irushika Thushari Fernando
Publikováno v: Food Science & Nutrition, 7(2):425-432
Food Science & Nutrition
Food Science & Nutrition, Vol 7, Iss 2, Pp 425-432 (2019)
This study investigated the effect of boiling on the inhibitory action of spices on digestive enzymes. Unboiled extracts of Trigonella foenum‐graecum (seed) (25.42%), Myristica fragrans (seed) (22.70%), and Cuminum cyminum (seed) (19.17%) showed si
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f71a82eb14ae6384b1cb5efcdf67f85
https://repository.publisso.de/resource/frl:6423710
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2
Comparison of the primary structures, cytotoxicities, and affinities to phospholipids of five kinds of cytotoxins from the venom of Indian cobra, Naja naja
Autor: Akihiko Moriyama, Yoshiyuki Suzuki, Kazumi Matsubara, Mieko Suzuki-Matsubara, Senarath B. P. Athauda
Publikováno v: Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology. 179:158-164
The molecular mechanism underlying the hemolytic and cytolytic processes of cobra cytotoxins (CTXs) is not yet fully elucidated. To examine this, we analyzed the amino acid sequences, hemolytic and cytotoxic activities, and affinities to phospholipid
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84b8ba50ab2956004307de90f8fea440
https://doi.org/10.1016/j.cbpc.2015.09.015
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3
Stability Profiles of Nepenthesin in Urea and Guanidine Hydrochloride: Comparison with Porcine Pepsin A
Autor: Kenji Takahashi, Yuya Metoki, Keiko Kubota, Chiaki Shibata, Senarath B. P. Athauda
Publikováno v: Bioscience, Biotechnology, and Biochemistry. 74:2323-2326
Nepenthesin, an aspartic endopeptidase from the pitcher fluid of Nepenthes, was found to be markedly less stable than porcine pepsin A when treated with urea or guanidine hydrochloride. This is in sharp contrast with its remarkably high pH/temperatur
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1a751581962ef2c8bd19217780e8e1a
https://doi.org/10.1271/bbb.100391
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4
Cathepsin L-like cysteine proteases from Brugia malayi: cDNA cloning and comparison with Caenorhabditis elegans
Autor: Tomohiko Azuma, Kenji Hodotsuka, Akiko Ukai, Kenji Takahashi, Hideshi Inoue, Hiroyuki Nomura, Senarath B. P. Athauda, Mitsuyo Takase
Publikováno v: Biomedical Research. 25:287-293
Proteases are thought to be potentially useful targets for developing medicines to control filariasis caused by parasitic nematodes. To screen cysteine proteases essential for viability of nematodes, fifteen cathepsin B/L-like genes of Caenorhabditis
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ec0b90656043411bdacd18282f44786a
https://doi.org/10.2220/biomedres.25.287
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5
Inhibition of Human Pepsin and Gastricsin by α2-Macroglobulin
Autor: Masaaki Nishigai, Senarath B. P. Athauda, Atsushi Ikai, Kenji Takahashi, Masanori Ukai, Hideo Arakawa
Publikováno v: Journal of Enzyme Inhibition and Medicinal Chemistry. 18:219-224
The inhibitory effects of human alpha2-macroglobulin (alpha2-M), a major plasma proteinase inhibitor, on human pepsin and gastricsin were investigated. The activities of pepsin and gastricsin towards a protein substrate (reduced and carboxymethylated
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::139f7d4861a033522195c249ed614816
https://doi.org/10.1080/1475636031000101246
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6
Two Distinct Types of Aspartic Proteases in the Filarial Parasite Brugia malayi: Molecular Cloning and Tissue Distribution
Autor: Hideshi Inoue, Hiroyuki Nomura, Kenji Takahashi, Senarath B. P. Athauda
Publikováno v: Biomedical Research. 24:269-276
The cDNAs coding for two distinct types of aspartic proteases, Bm-ASP-1 and Bm-ASP-2, were cloned from the parasitic nematode Brugia malayi, an important pathogen of human lymphatic filariasis, and their amino acid sequences (393 and 452 residues, re
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::43948fcbe5c5f17044e1f5d6572dc10b
https://doi.org/10.2220/biomedres.24.269
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7
Purification and Further Characterization of Enteropeptidase from Porcine Duodenum
Autor: Kazumasa Miki, Masao Ichinose, Hideshi Inoue, Masashi Matsushima, Masao Omata, Senarath B. P. Athauda, Yasuko Sakurai, Hisashi Ito, Kenji Takahashi, Yong-Tae Kim, Yuichi Tsuchiya, Takayuki Takahashi, Shinko Tsukada-Kato, Naohisa Yahagi
Publikováno v: Journal of Biochemistry. 125:947-951
Enteropeptidase [EC 3.4.21.9] is a membrane-bound serine endopeptidase present in the duodenum that converts trypsinogen to trypsin. We previously cloned the cDNA of the porcine enzyme and deduced its entire amino acid sequence [M. Matsushima et al.
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4513d8b7c179ee2a3607c638722e9ec4
https://doi.org/10.1093/oxfordjournals.jbchem.a022373
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8
Purification and Characterization of Turtle Pepsinogen and Pepsin
Autor: Akira Hirasawa, Senarath B. P. Athauda, Kenji Takahashi
Publikováno v: Journal of Biochemistry. 120:407-414
Pepsinogen was purified from the gastric mucosa of soft-shelled turtle (Trionyx sinensis) by a series of chromatographies on DEAE-cellulose, Sephadex G-100, and Q-Sepharose. Upon chromatography on Q-Sepharose, it was separated into nine isoforms. The
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b31edd8c4a10d658561789eefc86c623
https://doi.org/10.1093/oxfordjournals.jbchem.a021427
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10
Inhibition of Cathepsin E by a2-Macroglobulin and the Resulting Structural Changes in the Inhibitor1
Autor: Hideo Arakawa, Kenji Takahashi, Atsushi Ikai, Senarath B. P. Athauda, Masaaki Nishigai, Takayuki Takahashi
Publikováno v: The Journal of Biochemistry. 113:526-530
The activity of cathepsin E (M(r) approximately 80K), a dimeric aspartic proteinase with two active sites per molecule, toward a protein substrate (reduced and carboxymethylated ribonuclease A) was shown to be completely inhibited by alpha 2-macroglo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::637f22163f3e3e0bfa261970c7f4062c
https://doi.org/10.1093/oxfordjournals.jbchem.a124077
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