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ADP-ribosylation of a specific protein from isolated intact bull testis nuclei
M R Faraone Menella1, E Leone, M Malanga
1Dipartimento di Chimica Organica e Biologica, Facoltà di Scienze, Università di Napoli, Italy.
Biochimica Et Biophysica Acta
|April 28, 1988
Abstract:
ADP-ribosylation of a specific basic protein has been investigated in isolated intact bull testis nuclei incubated with NAD+. The electrophoretic mobility, molecular weight and amino-acid composition of the purified bull testis specific protein are similar to those of rat testis protein. About 1-5% of the total radioactivity incorporated in the 20% acid-insoluble fraction was associated with testis protein and was identified as ADP-ribose.