نتایج جستجو برای: subtilisin

تعداد نتایج: 2234  

Journal: :Neuroscience 2013
C M Forrest L G Darlington T W Stone

The serine protease subtilisin-A produces a long-term depression (LTD) of synaptic potentials in hippocampal slices which differs mechanistically from classical LTD. Since caspases have been implicated in hippocampal plasticity, this study examined a possible role for these enzymes in subtilisin-induced LTD. Subtilisin produced a concentration-dependent decrease in the size of field excitatory ...

Journal: :iranian journal of public health 0
h moallaei dept. of medical basic sciences sabzevar faculty of medical sciences, iran f zaini dept. of medical mycology & parasitology, school of public health, tehran university of medical scie s rezaie dept. of medical mycology & parasitology, school of public health, tehran university of medical scie f nourbakhsh division of molecular biology, dept. of medical mycology & parasitology, school of public health, te g larcher groupe d’etude des interaction hộte-parasite, upres-ea 3142, laboratorie de parsitologie-mycologie,

background: subtilisin -like proteases are the group of proteases including keratinases found in dermatophytes which de­graded keratin. determination of the proteases activity of trichophyton vanbreuseghemii isolates which were obtained from soil and clinical and soil isolates of microsporum gypseum in iran and characterization of their genome were aim of present study. methods: ezymatic activi...

Journal: :Biochemistry 2001
P A Alexander B Ruan S L Strausberg P N Bryan

Stability is a property of subtilisin which has proven particularly amenable to enhancement via random mutagenesis and screening, yet the effects of most stabilizing mutations are not understood in structural and energetic detail. This paper seeks to explain the longstanding observation that stabilizing mutations are usually calcium-dependent in their stabilizing effect, irrespective of their p...

Journal: :Biochemistry 1998
L Wang B Ruan S Ruvinov P N Bryan

The 77-amino acid pro-domain greatly accelerates the in vitro folding of subtilisin in a bimolecular reaction whose product is a tight complex between folded subtilisin and folded pro-domain. In this complex the pro-domain has a compact structure with a four-stranded antiparallel beta-sheet and two three-turn alpha-helixes. When isolated from subtilisin, however, the pro-domain is 97% unfolded ...

Journal: :JOURNAL OF THE BREWING SOCIETY OF JAPAN 1993

Journal: :Journal of Biological Chemistry 1972

Journal: :Journal of Biological Chemistry 1968

Journal: :Proceedings of the National Academy of Sciences 1973

Journal: :Journal of Biological Chemistry 1967

Journal: :Biochemistry 2004
Biao Ruan Kathryn E Fisher Patrick A Alexander Viktoriya Doroshko Philip N Bryan

Subtilisin was engineered into a highly specific, processing protease, and the subtilisin prodomain was coengineered into an optimized recognition sequence. This involved five steps. First, a robust subtilisin mutant was created, which could tolerate the subsequent mutations needed for high specificity. Second, the substrate binding pocket was mutated to increase its sequence selectivity. Third...

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