Purification and partial physical-chemical characterization of a new bovine trypsin proteoform (zeta-trypsin).

Autor: Cruz FT; Pos-Graduate Program of Biotechnology - Federal University of Espírito Santo, Vitória, ES, Brazil., Rosa DP; Pos-Graduate Program of Biochemistry - Federal University of Espírito Santo, Vitória, ES, Brazil., Vasconcelos AVB; Pos-Graduate Program of Biotechnology - Federal University of Espírito Santo, Vitória, ES, Brazil., de Oliveira JS; Department of Biochemistry and Immunology - Federal University of Minas Gerais, Belo Horizonte, MG, Brazil., Bleicher L; Department of Biochemistry and Immunology - Federal University of Minas Gerais, Belo Horizonte, MG, Brazil; Pos-Graduate at Biochemistry and Immunology - Federal University of Minas Gerais, Belo Horizonte, MG, Brazil., Santos AMC; Pos-Graduate Program of Biotechnology - Federal University of Espírito Santo, Vitória, ES, Brazil; Pos-Graduate Program of Biochemistry - Federal University of Espírito Santo, Vitória, ES, Brazil. Electronic address: alexandre.santos@ufes.br.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 May; Vol. 268 (Pt 2), pp. 131860. Date of Electronic Publication: 2024 Apr 24.
DOI: 10.1016/j.ijbiomac.2024.131860
Abstrakt: Recent advancements in enzyme research have unveiled a new proteoform of bovine trypsin, expanding our understanding of this well-characterized enzyme. While generally similar to other trypsins, this novel proteoform comprises three polypeptide chains, marking a significant difference in activity, kinetic properties, and conformational stability. Compared with the already known bovine trypsin proteoforms, the results showed a lower: activity, k cat and k cat .K M -1 and protein 'foldedness' ratio for the new proteoform. Molecular autolysis, a common feature in trypsin and chymotrypsin, has been explored through comparative physical chemistry properties with other proteoforms. This new proteoform of trypsin not only enriches the existing enzyme repertoire but also promises to shed light on the intricate physiological pathway for enzyme inactivation. Our results suggest that the new trypsin proteoform is one of the likely final pathways for enzyme inactivation in a physiological environment. This discovery opens up new avenues for further research into the functional implications of this new trypsin proteoform.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2024 Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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