TY  - JOUR
AU  - Rastegari, Ali Asghar
AU  - Buzari, Behnaz
AU  - Pavelkić, Vesna M.
AU  - Gopčević, Kristina
AU  - Petković, Marijana
AU  - Bordbar, Abdol-Khalegh
PY  - 2013
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/5664
AB  - The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated using differential scanning calorimetry (DSC), UV absorbance, polyacrylamide gel electrophoresis (PAGE) and MALDI-TOF MS methods. The two independent two-state transitions model with view of physiological function of pepsin was used for analyzing thermal denaturation curves. The transition temperature (T-m) values ranging from 305.15 to 319.15K for the first transition and from 322.15 to 349.15K for the second transition in the examined pH range implicating the higher stability at pH 4 are in good agreement with MALDI-TOF MS results. The corresponding maximum, Delta G degrees(25), was stability obtained at pH 4 with values of 65.3 kJ mol(-1). (C) 2013 Elsevier B.V. All rights reserved.
T2  - Thermochimica Acta
T1  - Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques
VL  - 568
SP  - 165
EP  - 170
DO  - 10.1016/j.tca.2013.06.030
ER  - 

@article{
author = "Rastegari, Ali Asghar and Buzari, Behnaz and Pavelkić, Vesna M. and Gopčević, Kristina and Petković, Marijana and Bordbar, Abdol-Khalegh",
year = "2013",
abstract = "The thermal stability of pepsin in a strong acid medium as a function of pH has been investigated using differential scanning calorimetry (DSC), UV absorbance, polyacrylamide gel electrophoresis (PAGE) and MALDI-TOF MS methods. The two independent two-state transitions model with view of physiological function of pepsin was used for analyzing thermal denaturation curves. The transition temperature (T-m) values ranging from 305.15 to 319.15K for the first transition and from 322.15 to 349.15K for the second transition in the examined pH range implicating the higher stability at pH 4 are in good agreement with MALDI-TOF MS results. The corresponding maximum, Delta G degrees(25), was stability obtained at pH 4 with values of 65.3 kJ mol(-1). (C) 2013 Elsevier B.V. All rights reserved.",
journal = "Thermochimica Acta",
title = "Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques",
volume = "568",
pages = "165-170",
doi = "10.1016/j.tca.2013.06.030"
}

Rastegari, A. A., Buzari, B., Pavelkić, V. M., Gopčević, K., Petković, M.,& Bordbar, A.. (2013). Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques. in Thermochimica Acta, 568, 165-170.
https://doi.org/10.1016/j.tca.2013.06.030

Rastegari AA, Buzari B, Pavelkić VM, Gopčević K, Petković M, Bordbar A. Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques. in Thermochimica Acta. 2013;568:165-170.
doi:10.1016/j.tca.2013.06.030 .

Rastegari, Ali Asghar, Buzari, Behnaz, Pavelkić, Vesna M., Gopčević, Kristina, Petković, Marijana, Bordbar, Abdol-Khalegh, "Thermal denaturation of pepsin at acidic media: Using DSC, MALDI-TOF MS and PAGE techniques" in Thermochimica Acta, 568 (2013):165-170,
https://doi.org/10.1016/j.tca.2013.06.030 . .