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ADP-ribosylation of a specific protein from isolated intact bull testis nuclei
- Source :
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 954:58-64
- Publication Year :
- 1988
- Publisher :
- Elsevier BV, 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.
- Subjects :
- Male
Biophysics
Biology
Testicle
Biochemistry
chemistry.chemical_compound
Structural Biology
Testis
medicine
Animals
Amino Acids
Molecular Biology
Cell Nucleus
Gel electrophoresis
Adenosine Diphosphate Ribose
Proteins
Molecular biology
Cell nucleus
medicine.anatomical_structure
chemistry
ADP-ribosylation
Cattle
NAD+ kinase
Testis-specific protein
PMSF
Protein Processing, Post-Translational
Spermatogenesis
Subjects
Details
- ISSN :
- 01674838
- Volume :
- 954
- Database :
- OpenAIRE
- Journal :
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Accession number :
- edsair.doi.dedup.....4759bdeb065c81faa5a715a2737b040b