Hsp70 from Cyprinion macrostomus macrostomus and Garra rufa obtuse Stability and stability dependent activity
Yazarlar (3)
Y. Tutar
Cumhuriyet Üniversitesi, Türkiye
Cumhuriyet Üniversitesi, Türkiye
K. A. Coskun
Cumhuriyet Üniversitesi Tip Fakültesi, Türkiye
Cumhuriyet Üniversitesi Tip Fakültesi, Türkiye
Dr. Öğr. Üyesi Lütfi TUTAR Kahramanmaras Sütçü Imam Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Biochemistry Moscow | ||
| Dergi ISSN | 0006-2979 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 05-2013 |
| Cilt / Sayı / Sayfa | 78 / 5 / 531–535 | DOI | 10.1134/S0006297913050118 |
| Makale Linki | http://link.springer.com/10.1134/S0006297913050118 | ||
| UAK Araştırma Alanları |
Moleküler Biyoloji ve Genetik
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| Özet |
| Two fish species, Cyprinion macrostomus macrostomus and Garra rufa obtuse, tolerate adverse conditions in the Kangal hot springs and cope with multiple stressors such as food deprivation, extreme temperature, toxins, protein degradation, hypoxia, and microbial damage. These fish have evolved strategies to counteract the stressors including the induction of heat shock proteins (Hsps). Hsps play an essential role in maintaining cellular homeostasis, and one of the key proteins in the mechanism is Hsp70. Hsp70 itself is exposed to the same stressors as all other proteins, and, hence, the stability of Hsp70 was investigated. For this purpose, Hsp70 ATPase activity was determined at different urea concentrations. It was found that the protein maintains considerable ATP hydrolysis activity at higher denaturant conditions. Temperature effects on the substrate peptide binding showed that Hsp70s bind prominently at … |
| Anahtar Kelimeler |
| aggregation | Hsp70 | stability |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| Scopus | 2 |
| Google Scholar | 3 |