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. 2019 Apr 16;9:6125. doi: 10.1038/s41598-019-42524-z

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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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Effect of auxiliary domains on prothrombin proteolysis by chymotrypsin. Chymotrypsin cleaves at W468 in the autolysis loop only when prothrombin assumes the open conformation (ΔLnk2, ΔLnk3; see also Fig. 2B). Upon removal of kringle-2 (ΔK2) and Lnk3 (ΔLnk3), chymotrypsin proteolysis leads to accumulation of 50 and 6 kDa species, due to the cleavage at W468, and two major bands at 30 and 5 kDa resulting from cleavage at L163 in Lnk2 and Y405 in the protease domain (see also Fig. 1C). Removal of the Gla domain (ΔGla), kringle-1 (ΔK1) or Lnk1 (ΔLnk1) makes prothrombin resistant to proteolytic attack. Chemical identities of the bands were verified by N-terminal sequencing. None of the gels were cropped and originals are available in the Supplementary Information as Fig. S3.