ADP-ribosylation of a specific protein from isolated intact bull testis nuclei.
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.
Faraone Menella
M R
MR
Dipartimento di Chimica Organica e Biologica, Facoltà di Scienze, Università di Napoli, Italy.
Leone
E
E
Malanga
M
M
Farina
B
B
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002467:Cell Nucleus / Q000032:analysis; D008297:Male; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D013737:Testis / Q000032:analysis*
D000596:Amino Acids; D011506:Proteins; D000246:Adenosine Diphosphate Ribose