Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

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

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 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/.

PMC Copyright notice

Exposure of the autolysis loop in the components of prothrombin activation as probed by limited proteolysis with chymotrypsin. After conversion of prothrombin (PT) to the active meizothrombin (MzT) or inactive prethrombin-1 (Pre1) and prethrombin-2 (Pre2) derivates, the autolysis loop becomes exposed and susceptible to chymotrypsin attack at W468. In the case of MzT, chymotrypsin cleaves additionally at Y277 and F281 in Lnk3, generating a 38 kDa species. Exposure of the autolysis loop reflects the open-closed equilibrium of prothrombin. The open conformation (mutant Y93A) is proteolytically attacked by chymotrypsin, but the closed form (mutant S101C/A470C) is not. All reactions were conducted in TBS buffer at 37 °C and analyzed by SDS-PAGE under non-reducing conditions. Chemical identities of the bands were verified by N-terminal sequencing (see Supplementary Table S1). None of the gels were cropped and originals are available in the Supplementary Information as Fig. S2.