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We began analyzing https://www.nature.com/articles/4400497, but it redirected us to https://www.nature.com/articles/4400497. The analysis below is for the second page.

Title[redir]:
Purification and catalytic properties of human caspase family members | Cell Death & Differentiation
Description:
Members of the caspase family of cysteine proteases are known to be key mediators of mammalian inflammation and apoptosis. To better understand the catalytic properties of these enzymes, and to facilitate the identification of selective inhibitors, we have systematically purified and biochemically characterized ten homologues of human origin (caspases 1–10). The method used for production of most of these enzymes involves folding of active enzymes from their constituent subunits which are expressed separately in E. coli, followed by ion exchange chromatography. In cases where it was not possible to use this method (caspase-6 and -10), the enzymes were instead expressed as soluble proteins in E. coli, and partially purified by ion exchange chromatography. Based on the optimal tetrapeptide recognition motif for each enzyme, substrates with the general structure Ac-XEXD-AMC were used to develop continuous fluorometric assays. In some cases, enzymes with virtually identical tetrapeptide specificities have kcat/Km values for fluorogenic substrates that differ by more than 1000-fold. Using these assays, we have investigated the effects of a variety of environmental factors (e.g. pH, NaCl, Ca2+) on the activities of these enzymes. Some of these variables have a profound effect on the rate of catalysis, a finding that may have important biological implications.

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Keywords {🔍}

nature, article, caspase, content, cell, enzymes, cookies, death, privacy, human, open, research, data, information, garciacalvo, access, advertising, differentiation, april, catalytic, properties, family, members, margarita, peterson, rasper, apoptosis, differ, january, author, permissions, optional, media, personal, parties, policy, journals, journal, original, paper, published, purification, erin, dita, john, vaillancourt, robert, zamboni, donald, nicholson,

Topics {✒️}

nature portfolio permissions reprints merck research laboratories privacy policy nature advertising general structure ac-xexd-amc social media author correspondence assemble α-acyloxyenamide electrophiles article garcia-calvo cell death differ personal data margarita garcia-calvo data protection permissions hela cell lysates privacy ac-tleu-asp journals search log explore content similar content european economic area ion exchange chromatography kcat/km values concerted domain motions article cite particulate danger signal red fluorescent probe invasive optical imaging accepting optional cookies caspase family enzymes involves folding mammalian inflammation manage preferences important biological implications https article luciferase-based inflammasome content robert zamboni & donald human origin journal publish apoptosis martin rights optional cookies //doi choices thornberry department essential cookies

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         description:Members of the caspase family of cysteine proteases are known to be key mediators of mammalian inflammation and apoptosis. To better understand the catalytic properties of these enzymes, and to facilitate the identification of selective inhibitors, we have systematically purified and biochemically characterized ten homologues of human origin (caspases 1â10). The method used for production of most of these enzymes involves folding of active enzymes from their constituent subunits which are expressed separately in E. coli, followed by ion exchange chromatography. In cases where it was not possible to use this method (caspase-6 and -10), the enzymes were instead expressed as soluble proteins in E. coli, and partially purified by ion exchange chromatography. Based on the optimal tetrapeptide recognition motif for each enzyme, substrates with the general structure Ac-XEXD-AMC were used to develop continuous fluorometric assays. In some cases, enzymes with virtually identical tetrapeptide specificities have kcat/Km values for fluorogenic substrates that differ by more than 1000-fold. Using these assays, we have investigated the effects of a variety of environmental factors (e.g. pH, NaCl, Ca2+) on the activities of these enzymes. Some of these variables have a profound effect on the rate of catalysis, a finding that may have important biological implications.
         datePublished:1999-04-09T00:00:00Z
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      headline:Purification and catalytic properties of human caspase family members
      description:Members of the caspase family of cysteine proteases are known to be key mediators of mammalian inflammation and apoptosis. To better understand the catalytic properties of these enzymes, and to facilitate the identification of selective inhibitors, we have systematically purified and biochemically characterized ten homologues of human origin (caspases 1â10). The method used for production of most of these enzymes involves folding of active enzymes from their constituent subunits which are expressed separately in E. coli, followed by ion exchange chromatography. In cases where it was not possible to use this method (caspase-6 and -10), the enzymes were instead expressed as soluble proteins in E. coli, and partially purified by ion exchange chromatography. Based on the optimal tetrapeptide recognition motif for each enzyme, substrates with the general structure Ac-XEXD-AMC were used to develop continuous fluorometric assays. In some cases, enzymes with virtually identical tetrapeptide specificities have kcat/Km values for fluorogenic substrates that differ by more than 1000-fold. Using these assays, we have investigated the effects of a variety of environmental factors (e.g. pH, NaCl, Ca2+) on the activities of these enzymes. Some of these variables have a profound effect on the rate of catalysis, a finding that may have important biological implications.
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