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PlcA (PI-PLC) |
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33-kDa, highly specific for PI, with a pH optimum between 5.5 and 6.5. Able to hydrolyze glycosyl PI(GPI)-anchored eukaryotic membrane proteins. ... |
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PlcA (PI-PLC) |
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33-kDa, highly specific for PI, with a pH optimum between 5.5 and 6.5. Able to hydrolyze glycosyl PI(GPI)-anchored eukaryotic membrane proteins. ... |
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PlcA (PI-PLC) |
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33-kDa, highly specific for PI, with a pH optimum between 5.5 and 6.5. Able to hydrolyze glycosyl PI(GPI)-anchored eukaryotic membrane proteins. ... |
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PlcA (PI-PLC) |
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33-kDa, highly specific for PI, with a pH optimum between 5.5 and 6.5. Able to hydrolyze glycosyl PI(GPI)-anchored eukaryotic membrane proteins. ... |
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PlcA (PI-PLC) |
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33-kDa, highly specific for PI, with a pH optimum between 5.5 and 6.5. Able to hydrolyze glycosyl PI(GPI)-anchored eukaryotic membrane proteins. ... |
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PlcB (PC-PLC) |
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Secreted as an inactive propeptide, activated on cleavage by the Mpl. Active between pH 5.0 and 8.0. Also called lecithinase, zinc-dependent enzyme. ... |
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PlcB (PC-PLC) |
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Secreted as an inactive propeptide, activated on cleavage by the Mpl. Active between pH 5.0 and 8.0. Also called lecithinase, zinc-dependent enzyme. ... |
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PlcB (PC-PLC) |
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Secreted as an inactive propeptide, activated on cleavage by the Mpl. Active between pH 5.0 and 8.0. Also called lecithinase, zinc-dependent enzyme. ... |
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PlcB (PC-PLC) |
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Secreted as an inactive propeptide, activated on cleavage by the Mpl. Active between pH 5.0 and 8.0. Also called lecithinase, zinc-dependent enzyme. ... |
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PlcB (PC-PLC) |
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Secreted as an inactive propeptide, activated on cleavage by the Mpl. Active between pH 5.0 and 8.0. Also called lecithinase, zinc-dependent enzyme. ... |
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