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Comparison of muralytic activities of OBPgp279, PVP-SE1gp146, 201φ2-1gp229, the catalytic domains of OBPgp279 (OBP127-327) and of 201φ2-1 (201φ2-175–260), with phage endolysins KZ144 and EL188.

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Figshare2015-12-02 更新2026-04-29 收录
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https://figshare.com/articles/dataset/_Comparison_of_muralytic_activities_of_OBPgp279_PVP_SE1gp146_201_2_1gp229_the_catalytic_domains_of_OBPgp279_OBP_127_327_and_of_201_966_2_1_201_966_2_1_75_8211_260_with_phage_endolysins_KZ144_and_EL188_/309131
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*[6] Briers et al.The muralytic activities of the endolysins were calculated from the slope of the best linear regression of the corresponding saturation curves, according to the definition for enzyme unit adapted from Briers and coworkers [11]. OM permeabilized P. aeruginosa PAO1 cell substrate resuspended in the optimal KH2PO4/K2HPO4 buffer (pH 7.2) was used to test the enzymatic activity. The endolysins were dialyzed against a PBS buffer (pH 7.4). Activity values of KZ144 and EL188 [6] were marked with an asterisk. R-square values for each slope are indicated between brackets. Constructs were ranked from the highest to the lowest muralytic activity.
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2015-12-02
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