Recombinant human carbonic anhydrase VII: Purification, characterization, inhibition, and molecular docking studies
Yazarlar (2)
Doç. Dr. Hatice Esra DURAN Kafkas Üniversitesi, Türkiye
Prof. Dr. Şükrü Beydemir Anadolu Üniversitesi, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY (Q2) | ||
| Dergi ISSN | 0885-4513 Dergi Bilgileri (2023) | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 02-2023 |
| Kabul Tarihi | 01-05-2022 | Yayınlanma Tarihi | 08-06-2022 |
| Cilt / Sayı / Sayfa | 70 / 1 / 415–428 | DOI | 10.1002/bab.2367 |
| Makale Linki | http://dx.doi.org/10.1002/bab.2367 | ||
| UAK Araştırma Alanları |
Tıbbi Biyokimya
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| Özet |
| Human carbonic anhydrase VII (hCA VII), a cytosolic enzyme, defends against oxidative stress by preventing reactive oxygen species from forming. In our study, first, hCA VII was cloned into Escherichia coli (One Shot Mach1‐T1R) strain by using cDNA of the human brain and successfully expressed. The integrity of the plasmid generated by colony PCR was checked, and after, for protein expression, the plasmid was transformed into E. coli BL21 (DE‐3) strain. hCA VII expression was observed after 6 h of isopropyl‐D‐1‐thiogalactopyranoside (IPTG) induction. The fusion protein containing hexahistidine (6xHis) was purified with 7.02 EU/mg of specific activity, had 48.07% of purification yield, and approximately 21‐folds using a ProbondTM nickel chelating resin affinity column. Then, both molecular mass determination and purity control of the purified recombinant enzyme was done by SDS‐PAGE (sodium dodecyl … |
| Anahtar Kelimeler |
| carbonic anhydrase | E | coli | enzyme catalysis | metalloenzymes | molecular docking | recombinant protein |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| Web of Science | 7 |
| Google Scholar | 7 |