Heterologous Expression and Molecular Cloning from Williamsia Marianensis
  
Yazarlar (4)
Alaa Kadhim Shareef Shareef
Prof. Dr. Belgin ERDEM Kırşehir Ahi Evran Üniversitesi, Türkiye
Ahmed Jasim Neamah
Ahmed Sadeq Habeeb Al-Adban
Çankırı Karatekin Üniversitesi, Türkiye
Makale Türü Özgün Makale (Ulusal alan endekslerinde (TR Dizin, ULAKBİM) yayınlanan tam makale)
Dergi Adı International Journal of Computational and Experimental Science and Engineering
Dergi ISSN 2149-9144 Scopus Dergi
Dergi Tarandığı Indeksler TR DİZİN
Makale Dili İngilizce Basım Tarihi 09-2022
Cilt / Sayı / Sayfa 8 / 3 / 69–73 DOI 10.22399/ijcesen.1133001
Makale Linki https://dergipark.org.tr/en/download/article-file/2495835
Özet
The majority of therapy methods include downsides and limits. As a result, many researchers are focused on developing effective remedies. Therapeutic peptides, like proteins and antibodies, are a potential class of medications that have a number of advantages over traditional pharmaceuticals. Williamson marianensis-produced cholesterol oxididase has been demonstrated to have medicinal value. Using PCR and primers specific to an expression vector (pET28b), we were able to clone the cholestrol oxidase gene and express it in E. coli (BL-21/DE3) Rosetta following identification with IPTG. Genscript Corporation in the United States sequenced gyncholestrol oxidase (500 bp) to create a cox sequence, which was then submitted for synthesis. pET 28a(+) cox william showed a twofold restriction digestion pattern. The pattern was made up of two strands: one was a carrier plasmid (4200 bp) and the other was a 2800 base pair strand that contained the cholesterol oxidase gene. The cholesterol oxidase gene was successfully cloned and expressed as a consequence. Williamson marianensis-derived cholesterol oxidase will be exploited in future medicinal results.
Anahtar Kelimeler
Human infections | Williamson | PCR
BM Sürdürülebilir Kalkınma Amaçları
Atıf Sayıları
TRDizin 1
Heterologous Expression and Molecular Cloning from Williamsia Marianensis

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