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. 2021 Mar 16;8:618068. doi: 10.3389/fmolb.2021.618068

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Copyright © 2021 Narkhede, Gautam, Hsu, Rodriguez, Zewde, Harrison, Arantes, Gaieb, Gorham, Kieslich, Morikis, Sahu and Palermo.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Cofactor activity of human factor H for human and bovine C3b. (A) Analysis of cofactor activity by SDS-PAGE gel analysis. C3b (human or bovine) was mixed with human factor H and factor I (human or bovine), incubated at 37 °C for the indicated time, and examined for C3b cleavage (α′-chain cleavage) by running the reaction mix on SDS-PAGE. (B) The amount of α′-chain at different time points was quantitated densitometrically and plotted against time. (C) Relative cofactor activity of factor H against human and bovine C3b in the presence of human or bovine factor I. The molar concentration of the complement components used in the cofactor assay was: 758 nM Hu/Bo C3b, 11 nM Hu/Bo factor I and 473 nM Hu factor H.