Zobrazeno 1 - 10
of 157
pro vyhledávání: '"Thermitase"'
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 1987 Nov 01. 84(21), 7508-7512.
Externí odkaz:
https://www.jstor.org/stable/30849
Publikováno v:
Protein Expression and Purification. 92:148-155
Thermitase (EC 3.4.21.66) is a thermostable endo-protease with the ability to convert various food relevant substrates into low-molecular weight peptides. A thermitase produced by Laceyella sacchari strain DSM43353 was found to have a mature amino ac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c70ca1b36d8b219ee868b41e109781e
https://doi.org/10.1016/j.pep.2013.09.009
https://doi.org/10.1016/j.pep.2013.09.009
Autor:
Klaus D. Wutzke
Publikováno v:
Isotopes in Environmental and Health Studies. 48:239-258
Our research group of the Children's Hospital of the University of Rostock (Rostock group) has long-time experience in (15)N-labelling and in using yeast protein and its hydrolysates for tracer kinetic studies to evaluate parameters of the whole-body
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8469449424a67d6bb8ee1992be4bbd01
https://doi.org/10.1080/10256016.2012.662971
https://doi.org/10.1080/10256016.2012.662971
Publikováno v:
International Journal of Peptide and Protein Research. 23:134-141
The influence of chloromethyl ketones and methyl ketones of N-acylated peptides on the thermal denaturation of thermitase was investigated in the presence and the absence of calcium ions. The chloromethyl ketone derivatives are known to react irrever
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8402354a199f1199735bb878e7c7978
https://doi.org/10.1111/j.1399-3011.1984.tb02703.x
https://doi.org/10.1111/j.1399-3011.1984.tb02703.x
Publikováno v:
Journal of Molecular Graphics and Modelling. 25:176-185
The role of the primary binding residue (P1) in complexes between three different subtilases (subtilisin Carlsberg, thermitase and proteinase K) and their canonical protein inhibitor eglin c have been studied by free energy calculations. Based on the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0a12edddfa16f4251d859cff97d6d326
https://doi.org/10.1016/j.jmgm.2005.11.005
https://doi.org/10.1016/j.jmgm.2005.11.005
Publikováno v:
FEBS Journal. 272:832-845
The crystal structure of a subtilisin-like serine proteinase from the psychrotrophic marine bacterium, Vibrio sp. PA-44, was solved by means of molecular replacement and refined at 1.84 A. This is the first structure of a cold-adapted subtilase to be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::25e6ea155e67761ac0dec7c9fcdcb406
https://doi.org/10.1111/j.1742-4658.2005.04523.x
https://doi.org/10.1111/j.1742-4658.2005.04523.x
Akademický článek
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Autor:
L. I. Kostina, A. L. Mikhailova, Zalunin Ia, Galina G. Chestukhina, L. A. Ganushkina, L. P. Revina
Publikováno v:
Biochemistry (Moscow). 69:181-187
Subtilisin hydrolyzes Cry11A endotoxin (of 70 kD) produced by Bacillus thuringiensis ssp. israelensis to fragments of 33- and 36-kD, which correspond to N- and C-terminal halves of the endotoxin molecule. Thermitase (a serine protease from Thermoacti
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cabcd91f3af2bdd506b2f32c48debdf2
https://doi.org/10.1023/b:biry.0000018949.70836.dc
https://doi.org/10.1023/b:biry.0000018949.70836.dc
Autor:
Vichien Kitpreechavanich, Sukhumaporn Sukkhum, Shinji Tokuyama, Narisara Maneewong, Srisuda Hanphakphoom
Publikováno v:
The Journal of general and applied microbiology. 60(1)
Eleven strains of poly(L-lactide) (PLLA)-degrading thermophilic bacteria were isolated from forest soils and selected based on clear zone formation on an emulsified PLLA agar plate at 50°C. Among the isolates, strain LP175 showed the highest PLLA-de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bbb7c145b15ba503a62f689840f3bcf5
https://pubmed.ncbi.nlm.nih.gov/24646757
https://pubmed.ncbi.nlm.nih.gov/24646757
Publikováno v:
Biochemical Journal. 350:321-328
Ak.1 protease, a thermostable subtilisin isolated originally from Bacillus st. Ak.1, was purified to homogeneity from the Escherichia coli clone PB5517. It is active against substrates containing neutral or hydrophobic branched-chain amino acids at t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9f6ea4a245a0ca5e5db1e2112f484e52
https://doi.org/10.1042/bj3500321
https://doi.org/10.1042/bj3500321