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A protein kinase (EC 2.7.1.37) was purified 2000-fold, from the soluble protein fraction of human spleen cells, using ion-exchange chromatography, ammonium sulfate fractionation, and gel filtration. This rapid procedure yielded 30% of the initial act
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https://explore.openaire.eu/search/publication?articleId=od_____10561::0877e7316cd1a7353c0a669ec1ee9524
http://olympias.lib.uoi.gr/jspui/handle/123456789/7473
http://olympias.lib.uoi.gr/jspui/handle/123456789/7473
Increased levels of soluble activity of all three enzymes involved in polyadenylic acid metabolism were measured in PHA-stimulated versus normal lymphocytes. Poly(A)-polymerase and poly(A)-exonuclease values increased significantly (from 25.7 +/- 4.2
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_____10561::d012c0e3dd0acb9b40ca969bcea2c77d
http://olympias.lib.uoi.gr/jspui/handle/123456789/7462
http://olympias.lib.uoi.gr/jspui/handle/123456789/7462
Autor:
Gounaris A; Department of Biochemistry, Papanikolaou Research Center, Hellenic Anticancer Institute, Greece., Trangas TT, Tsiapalis CM
Publikováno v:
Archives of biochemistry and biophysics [Arch Biochem Biophys] 1987 Dec; Vol. 259 (2), pp. 473-80.
Publikováno v:
Molecular and cellular biochemistry [Mol Cell Biochem] 1987 May; Vol. 75 (1), pp. 33-42.