TR Dizin İndeksli Yayınlar / TR Dizin Indexed Publications Collection

Permanent URI for this collectionhttps://hdl.handle.net/11147/7149

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  • Article
    Citation - Scopus: 2
    Identification of Potato Y Potyvirus (pvy°) Resistance in Wild and Cultivated Tomatoes
    (Türkiye Klinikleri Journal of Medical Sciences, 2009) Çelebi Toprak, Fevziye; Barutçu, Eminur; Frary, Anne; Doğanlar, Sami
    Potato Y potyvirus (PVY) is an important plant pathogen worldwide that infects and causes yield losses in the family Solanaceae including potato (Solarium tuberosum), pepper (Capsicum spp.), tomato (S. lycopersicum), and tobacco (Nicotiana tabacum). In this study, 20 different tomato accessions representing 6 different species were mechanically inoculated with PVY°. The plants were scored visually for symptoms and then tested for presence of the virus 2-4 weeks after inoculation by ELISA. The results were variable. Most wild species of tomato sustained PVY° replication in inoculated leaves. Some of the wild species showed an immune response, while some became systemically infected. Inoculation and analysis of F2 populations suggested that the resistance is controlled by a single recessive gene in different wild species.
  • Article
    Citation - WoS: 11
    Citation - Scopus: 16
    Partial Purification of Hen Egg White Lysozyme by Ethanol Precipitation Method and Determination of the Thermal Stability of Its Lyophilized Form
    (Türkiye Klinikleri Journal of Medical Sciences, 2007) Gemili, Seyhun; Umdu, Emin Selahattin; Yaprak, Nilgün; Üstok, Fatma Işık; Yener, Fatih Yalçın Güneş; Mecitoğlu Güçbilmez, Çiğdem; Altınkaya, Sacide; Yemenicioğlu, Ahmet
    Lysozyme was partially purified from hen egg white by precipitation of non-lysozyme protein impurities during incubation in the prence of ethanol. The thermal stability of the obtained partially purified enzyme was also characterized. The incubation of diluted egg white for 2-8 h in the presence of 20% ethanol was not very effective for the partial purification of lysozyme by precipitation of major egg white proteins; however, 4- to 6-h or 6-h to 8-h incubation of diluted egg white in the presence of 30% and 40% ethanol could be employed more effectively for partial purification of lysozyme. Without applying the incubation period, the highest specific activity was obtained by the treatment of egg white with 40% ethanol. Thus, ethanol at this concentration could be used for a continuous process of partial purification. For batch lysozyme purification, on the other hand, incubation in the presence of 30% ethanol was more appropriate. The activities and protein contents of dialyzed and lyophilized enzymes obtained by 6 h-incubation in the presence of 20%, 30%. and 40% ethanol precipitations were 1878, 6669, and 6115 U/mg powder, and 0.98, 0.90, and 0.93 mg protein per mg powder, respectively. The ranges of thermal inactivation parameters, such as D (D80°C = 29.2-59 min, D90°c = 8.8-21 min) and z (Z80-90°c = 17.4-22.3 °C) values of the enzyme, clearly indicated the moderate and variable heat stability of lyophilized lysozymes obtained from different batches of egg white.