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. 2021 Apr 21;11:8648. doi: 10.1038/s41598-021-87980-8

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© The Author(s) 2021

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Kinetic analysis of purified SSTI. Noncompetitive (mixed) type of inhibition of bovine trypsin (A) Michaelis–Menten kinetics of bovine trypsin in presence and in absence of SSTI. (B) Lineweaver–Burk plot of 1/[V] versus 1/[S] of bovine trypsin in presence and in absence of SSTI. (C) Dixon’s plot of 1/[V] versus [I] of bovine trypsin in presence of different concentrations of SSTI at two different concentrations of BApNA. The Ki value for SSTI was 16.6 × 10⁻⁸ M. (D) Interaction by Isothermal titration of purified SSTI with bovine trypsin.