In this paper an (ADPribosyl)ation system in Saccharomyces cerevisiae was characterized .Yeast (ADPribosyl)ating enzyme is a protein of 80-90 kDa, as determined by electrophoresis on polyacrylamide gel in sodium dodecyl sulphate, followed by immunoblotting with antibodies against anti-poly(ADPribose) polymerase catalytic site. It synthesizes products, that, after digestion with phosphodiesterase, co-migrates mainly with phosphoribosyl adenosine monophosphate after thin layer chromatography on silica gel plate.
YEAST (ADPRIBOSYL)ATION: REVISITING A CONTROVERSIAL QUESTION / FARAONE MENNELLA, MARIA ROSARIA; DE MAIO, Anna; A., Petrella; E., Syntichaki; A. M., Kerbalaeva; S. M., Nasmetova; T. G., Goulyamova; Farina, Benedetta. - In: JOURNAL OF CELLULAR BIOCHEMISTRY. - ISSN 0730-2312. - ELETTRONICO. - 94 (6),:(2005), pp. 1258-1266.
YEAST (ADPRIBOSYL)ATION: REVISITING A CONTROVERSIAL QUESTION.
FARAONE MENNELLA, MARIA ROSARIA;DE MAIO, ANNA;FARINA, BENEDETTA
2005
Abstract
In this paper an (ADPribosyl)ation system in Saccharomyces cerevisiae was characterized .Yeast (ADPribosyl)ating enzyme is a protein of 80-90 kDa, as determined by electrophoresis on polyacrylamide gel in sodium dodecyl sulphate, followed by immunoblotting with antibodies against anti-poly(ADPribose) polymerase catalytic site. It synthesizes products, that, after digestion with phosphodiesterase, co-migrates mainly with phosphoribosyl adenosine monophosphate after thin layer chromatography on silica gel plate.| File | Dimensione | Formato | |
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