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. 2019 Mar 13;9:4340. doi: 10.1038/s41598-019-40983-y

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Purified fibrinogen concentration-dependently reduces binding of recombinant MMP-2 to gelatin. Top left: Strategy for assessing a lack of binding of MMP-2 to gelatin in the presence or absence of FBG. Top right: Gelatin binding assay followed by gelatin zymography shows an increase in gelatinolytic activity of MMP-2 remaining in the gelatin-unbound fraction with increasing FBG concentration. Gelatin zymogram showing gelatinolytic activity of MMP-2 in the gelatin-unbound fraction for varying [FBG]: [MMP-2] ratios (0: 1 to 800: 1). Uncropped gel is presented in Supplementary Fig. S7. Bottom: Quantitation of the intensities of the lysis bands in the gelatin zymogram (left) by densitometry. Relative intensity for each band was calculated by dividing the absolute intensity of each band by the absolute intensity of the band at [FBG] = 0 μM ([FBG]: [MMP-2] = 0:1).