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Cloning And Sequencing Of Coat Protein Gene Of Zucchini Yellow Mosaic Virus Isolated From Squash And Muskmelon In Turkey, Meryem Özer, Hi̇kmet Murat Si̇pahi̇oğlu, Mustafa Usta, Hakan Fi̇dan
Cloning And Sequencing Of Coat Protein Gene Of Zucchini Yellow Mosaic Virus Isolated From Squash And Muskmelon In Turkey, Meryem Özer, Hi̇kmet Murat Si̇pahi̇oğlu, Mustafa Usta, Hakan Fi̇dan
Turkish Journal of Biology
The coat protein (CP) genes of the genomic RNA of 2 severe Turkish isolates of Zucchini yellow mosaic virus (ZYMV) from squash and muskmelon [ZYMV-Adana (Ad) and ZYMV-Ahlat (Ah), respectively] were cloned, and their complete nucleotide sequences and deduced amino acids were determined. The analysis revealed that both Turkish ZYMV-CP genes contained 837 nucleotides encoded for a CP of about 31.2 kDa. Phylogenetic trees based on nucleic acid sequences were constructed by the neighbor joining and unweighted pair group mean arithmetic (UPGMA) methods with 100 bootstrap replicates. A high degree of homology was detected between the 2 Turkish isolates on …
Alkaline Protease Production Of Bacillus Cohnii Apt5, Ni̇lgün Teki̇n, Arzu Çöleri̇ Ci̇han, Zeki̇ye Serpi̇l Takaç, Canan Yağci Tüzün, Kenan Tunç, Cumhur Çökmüş
Alkaline Protease Production Of Bacillus Cohnii Apt5, Ni̇lgün Teki̇n, Arzu Çöleri̇ Ci̇han, Zeki̇ye Serpi̇l Takaç, Canan Yağci Tüzün, Kenan Tunç, Cumhur Çökmüş
Turkish Journal of Biology
An obligate alkaliphilic Bacillus strain was isolated from a soil sample and identified as Bacillus cohnii APT5 based upon phylogenetic and phenotypic analyses. The optimum growth pH of B. cohnii APT5 was 10.0. B. cohnii APT5 was also found capable of producing an extracellular alkaline protease that showed optimum activity (693,318 U/min) at 50 °C and pH 11.0 when grown in a medium containing casein. The enzyme was partially purified 3.22-fold with a yield of 78.74% after acetone precipitation and cation exchange column chromatography, respectively. The partially purified enzyme maintained its activity when incubated at 50 °C for 2 h. …