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. 2017 Mar 21;18(3):670. doi: 10.3390/ijms18030670

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© 2017 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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Interaction studies between crARC, crCytb5-1 and crCytb5-R. The SEC profiles of the indicated samples are shown. In these experiments, the proteins crARC, crCytb5-1 and crCytb5-R were loaded separately and then together in different combinations to observe the appearance of new peaks. (a) The proteins loaded separately; (b) crARC, with crCytb5-1, and crARC with crCytb5-R; (c) The crCytb5-1 protein with crCytb5-R; (d) The proteins crARC plus, crCytb5-1 and crCytb5-R together; (e) Calibration curve obtained using the Mw protein marker; the graph represents the Mw versus the logarithm of the elution volume. The absorbance was measured at 280 nm; (f) sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis of the protein peak indicated with the symbol * obtained in the SEC.