التفاصيل البيبلوغرافية
العنوان: |
Modulation of global stability, ligand binding and catalytic properties of trypsin by anions |
المؤلفون: |
Dušeková, Eva, Garajová, Katarína, Yavaser Rukiye, Sedláková, Dagmar, Dzurillová, Veronika, Kulik, Natalia, Shaposhnikova, Anastasiia, Fadaei, Fatemeh, Tomková, Mária, Minofar, Babak, Sedlák, Erik |
المساهمون: |
Erik Sedlák |
المصدر: |
Biophysical Chemistry, 288, 106856, (2022-07-13) |
بيانات النشر: |
Zenodo |
سنة النشر: |
2022 |
المجموعة: |
Zenodo |
مصطلحات موضوعية: |
Hofmeister effect, macromolecular rate theory, enzyme dynamics, enzyme activity, serine protease |
الوصف: |
Specific salts effect is well-known on stability and solubility of proteins, however, relatively limited knowledge is known regarding the effect on catalytic properties of enzymes. Here, we examined the effect of four sodium anions on thermal stability and catalytic properties of trypsin and binding of the fluorescent probe, p-aminobenzamidine (PAB), to the enzyme. We show that the specific anions effect on trypsin properties agrees with the localization of the anions in the Hofmeister series. Thermal stability of trypsin, Tm, the affinity of the fluorescent probe to the binding site, Kd, and the rate constant, kcat, of trypsin-catalyzed hydrolysis of the substrate N-benzoyl-L-arginine ethyl ester (BAEE) increase with increasing kosmotropic character of anions in the order: perchlorate ; Slovak Research and Development Agency through the project APVV-20-0340 and by the grant agency of the Ministry of Education, Science, Research, and Sport of the Slovak Republic (grant no. VEGA 1/0074/22) the project implementation: Open scientific community for modern interdisciplinary research in medicine (Acronym: OPENMED), ITMS2014+: 313011V455 supported by the Operational Programme Integrated Infrastructure, funded by the ERDF the project "e-Infrastruktura CZ" (e-INFRA LM2018140) provided within the program Projects of Large Research, Development and Innovations Infrastructures and the grant GAČR 21-15936S from the Czech Science Foundation |
نوع الوثيقة: |
report |
اللغة: |
unknown |
Relation: |
https://www.sciencedirect.com/science/article/pii/S0301462222000679; https://zenodo.org/communities/pavol-jozef-safarik-university-in-kosice-slovakia; https://zenodo.org/communities/eu; https://doi.org/10.1016/j.bpc.2022.106856; oai:zenodo.org:7110517 |
DOI: |
10.1016/j.bpc.2022.106856 |
الاتاحة: |
https://doi.org/10.1016/j.bpc.2022.106856 |
Rights: |
info:eu-repo/semantics/openAccess ; Creative Commons Attribution 4.0 International ; https://creativecommons.org/licenses/by/4.0/legalcode |
رقم الانضمام: |
edsbas.C29BA287 |
قاعدة البيانات: |
BASE |