Structure carboxyl-terminale des ATP:l-arginine phosphotransferases de poids moleculaire 43 000 (Homarus vulgaris) et 86 000 (Sipunculus nudus)
- 23 December 1969
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure
- Vol. 194 (2) , 540-547
- https://doi.org/10.1016/0005-2795(69)90116-0
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Étude de la conformation de diverses phosphagène phosphotransférases par dispersion optique rotatoireBiochimica et Biophysica Acta (BBA) - Protein Structure, 1969
- L'ATP : L‐arginine phosphotransférase de poids moléculaire élevéEuropean Journal of Biochemistry, 1969
- Interaction des ATP:Guanidine phosphotransférases avec leurs substrats, étudiée par spectrophotometrie différentielleBiochimica et Biophysica Acta (BBA) - Enzymology, 1968
- Studies on Adenosine Triphosphate Transphosphorylases. V. Studies on the Polypeptide Chains of the Crystalline Adenosine Triphosphate-Creatine Transphosphorylase from Rabbit Skeletal Muscle*Biochemistry, 1967
- A reinvestigation of the hydrazinolytic procedure for the determination of C-terminal amino acidsArchives of Biochemistry and Biophysics, 1967
- Composition en acides amines de l'ATP: l-arginine phosphotransferase cristalliseeBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1966
- Comparaison des poids moleculaires des ATP:guanidino phosphotransferasesBiochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation, 1965
- Studies on Adenosine Triphosphate TransphosphorylasesPublished by Elsevier ,1964