Lah, Jurij

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2a48ae8b-a758-4100-8207-9ac48d6b9fbf
  • Lah, Jurij (2)
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Author's Bibliography

Isolation, identification, and stability of Ficin 1c isoform from fig latex

Milošević, Jelica; Vrhovac, Lidija; Đurković, Filip T.; Janković, Brankica; Malkov, Saša; Lah, Jurij; Polović, Natalija

(Royal Society of Chemistry, 2020) 

TY  - JOUR
AU  - Milošević, Jelica
AU  - Vrhovac, Lidija
AU  - Đurković, Filip T.
AU  - Janković, Brankica
AU  - Malkov, Saša
AU  - Lah, Jurij
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4265
AB  - Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.
PB  - Royal Society of Chemistry
T2  - New Journal of Chemistry
T1  - Isolation, identification, and stability of Ficin 1c isoform from fig latex
VL  - 44
IS  - 36
SP  - 15716
EP  - 15723
DO  - 10.1039/D0NJ02938F
ER  - 
@article{
author = "Milošević, Jelica and Vrhovac, Lidija and Đurković, Filip T. and Janković, Brankica and Malkov, Saša and Lah, Jurij and Polović, Natalija",
year = "2020",
abstract = "Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.",
publisher = "Royal Society of Chemistry",
journal = "New Journal of Chemistry",
title = "Isolation, identification, and stability of Ficin 1c isoform from fig latex",
volume = "44",
number = "36",
pages = "15716-15723",
doi = "10.1039/D0NJ02938F"
}
Milošević, J., Vrhovac, L., Đurković, F. T., Janković, B., Malkov, S., Lah, J.,& Polović, N.. (2020). Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry
Royal Society of Chemistry., 44(36), 15716-15723.
https://doi.org/10.1039/D0NJ02938F
Milošević J, Vrhovac L, Đurković FT, Janković B, Malkov S, Lah J, Polović N. Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry. 2020;44(36):15716-15723.
doi:10.1039/D0NJ02938F .
Milošević, Jelica, Vrhovac, Lidija, Đurković, Filip T., Janković, Brankica, Malkov, Saša, Lah, Jurij, Polović, Natalija, "Isolation, identification, and stability of Ficin 1c isoform from fig latex" in New Journal of Chemistry, 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F . .
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Isolation, identification, and stability of Ficin 1c isoform from fig latex

Milošević, Jelica; Vrhovac, Lidija; Đurković, Filip T.; Janković, Brankica; Malkov, Saša; Lah, Jurij; Polović, Natalija

(Royal Society of Chemistry, 2020) 

TY  - JOUR
AU  - Milošević, Jelica
AU  - Vrhovac, Lidija
AU  - Đurković, Filip T.
AU  - Janković, Brankica
AU  - Malkov, Saša
AU  - Lah, Jurij
AU  - Polović, Natalija
PY  - 2020
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/4264
AB  - Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.
PB  - Royal Society of Chemistry
T2  - New Journal of Chemistry
T1  - Isolation, identification, and stability of Ficin 1c isoform from fig latex
VL  - 44
IS  - 36
SP  - 15716
EP  - 15723
DO  - 10.1039/D0NJ02938F
ER  - 
@article{
author = "Milošević, Jelica and Vrhovac, Lidija and Đurković, Filip T. and Janković, Brankica and Malkov, Saša and Lah, Jurij and Polović, Natalija",
year = "2020",
abstract = "Latex of common fig (Ficus carica) is a rich protein source with a high level of proteolytic activity contributing to its defensive role. The divergent group of cysteine proteases known as ficin (EC 3.4.22.3) represents the majority of latex protein content and shows activity towards fig parasites. Both classical and novel biochemical techniques suggest the intricate pattern of ficin expression and activity profiles. Even though structurally related, different ficin isoforms show some differences in pI values enabling their separation using ion-exchangers. A single alkaline isoform was purified and identified based on the available transcriptomic data as Ficin 1c. This isoform shows both general proteolytic and gelatinolytic activity suggesting a biological role in the degradation of a broad range of natural substrates. The insight into the Ficin 1c structure also provided some functional clues. The secondary structure content and the overall fold are similar to related proteases of the same and other plant sources resulting in similar unfolding routes. Stability assessment of Ficin 1c in comparison to ficin isoform mixture showed that isoform diversity might lead to increased protease stability.",
publisher = "Royal Society of Chemistry",
journal = "New Journal of Chemistry",
title = "Isolation, identification, and stability of Ficin 1c isoform from fig latex",
volume = "44",
number = "36",
pages = "15716-15723",
doi = "10.1039/D0NJ02938F"
}
Milošević, J., Vrhovac, L., Đurković, F. T., Janković, B., Malkov, S., Lah, J.,& Polović, N.. (2020). Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry
Royal Society of Chemistry., 44(36), 15716-15723.
https://doi.org/10.1039/D0NJ02938F
Milošević J, Vrhovac L, Đurković FT, Janković B, Malkov S, Lah J, Polović N. Isolation, identification, and stability of Ficin 1c isoform from fig latex. in New Journal of Chemistry. 2020;44(36):15716-15723.
doi:10.1039/D0NJ02938F .
Milošević, Jelica, Vrhovac, Lidija, Đurković, Filip T., Janković, Brankica, Malkov, Saša, Lah, Jurij, Polović, Natalija, "Isolation, identification, and stability of Ficin 1c isoform from fig latex" in New Journal of Chemistry, 44, no. 36 (2020):15716-15723,
https://doi.org/10.1039/D0NJ02938F . .
11
2
8
10