A novel mechanism of “metal gel-shift” by histidine-rich Ni-binding Hpn
نویسندگان
چکیده
23 Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) is a universally 24 used method for determining approximate molecular weight (MW) in protein research. 25 Migration of protein that does not correlate with formula MW, termed " gel shifting " appears 26 to be common for histidine-rich proteins but not yet studied in detail. We investigated " gel 27
منابع مشابه
A novel mechanism of “metal gel-shift” by histidine-rich Ni2+-binding Hpn protein from Helicobacter pylori strain SS1
Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) is a universally used method for determining approximate molecular weight (MW) in protein research. Migration of protein that does not correlate with formula MW, termed "gel shifting" appears to be common for histidine-rich proteins but not yet studied in detail. We investigated "gel shifting" in Ni2+-binding histidine-rich H...
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