Leucyl-tRNA synthetase from Thermus thermophilus. Purification and some properties of the crystallizing enzyme

Leucyl-tRNA synthetase from Thermus thermophilus (LeuRSTT) was purified to homogeneity using a five-step purification procedure. The enzyme was characterized and crystallized. Molecular mass determinations of the native and denatured proteins indicate monomeric structure of LeuRSTT with the molecula...

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Бібліографічні деталі
Дата:2001
Автори: Yaremchuk, A.D., Gudzera, O.I., Egorova, S.P., Rozhko, D.I., Kriklivy, I.A., Tukalo, M.A.
Формат: Стаття
Мова:English
Опубліковано: Інститут молекулярної біології і генетики НАН України 2001
Назва видання:Біополімери і клітина
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Онлайн доступ:http://dspace.nbuv.gov.ua/handle/123456789/155227
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Назва журналу:Digital Library of Periodicals of National Academy of Sciences of Ukraine
Цитувати:Leucyl-tRNA synthetase from Thermus thermophilus. Purification and some properties of the crystallizing enzyme / A.D. Yaremchuk, O.I. Gudzera, S.P. Egorova, D.I. Rozhko, I.A. Kriklivy, M.A. Tukalo // Біополімери і клітина. — 2001. — Т. 17, № 3. — С. 216-220. — Бібліогр.: 11 назв. — англ.

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Digital Library of Periodicals of National Academy of Sciences of Ukraine
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Резюме:Leucyl-tRNA synthetase from Thermus thermophilus (LeuRSTT) was purified to homogeneity using a five-step purification procedure. The enzyme was characterized and crystallized. Molecular mass determinations of the native and denatured proteins indicate monomeric structure of LeuRSTT with the molecular mass of about 101 kDa. The protein obtained is remarkably thermostable and retains 97 % of its initial aminoacylation activity after 1 hour of incubation at 88 °C. Crystals of LeuRSTT were obtained from ammonium sulfate solution by the vapour diffusion techniques. The crystals quality was improved by crystallization from the precipitate.