Using flame atomic absorption spectrometry the tight association of zinc to three different purified 5′-nucleotidases at a molar ratio of 2 could be proven. These 5′-nucleotides purified from bull seminal plasma (BSP), chicken gizzard (CG) and snake venom (SV) are thus zinc metalloproteins. Removal of zinc results in the loss of their AMPase activity, which could be fully restored after readdition of zinc at a molar ratio of 2, for BSP and CG, and 1.5, for SV 5′-nucleotidase. Reactivation of their AMPase activity after the removal of zinc could also be obtained by addition of cobalt and copper ions, which were found to also bind with a molar ratio of 2 to the three 5′-nucleotidases tested. © 1990.
5′-Nucleotidase from bull seminal plasma, chicken gizzard and snake venom is a zinc metalloprotein
FINI, Carlo;PALMERINI, Carlo Alberto;
1990
Abstract
Using flame atomic absorption spectrometry the tight association of zinc to three different purified 5′-nucleotidases at a molar ratio of 2 could be proven. These 5′-nucleotides purified from bull seminal plasma (BSP), chicken gizzard (CG) and snake venom (SV) are thus zinc metalloproteins. Removal of zinc results in the loss of their AMPase activity, which could be fully restored after readdition of zinc at a molar ratio of 2, for BSP and CG, and 1.5, for SV 5′-nucleotidase. Reactivation of their AMPase activity after the removal of zinc could also be obtained by addition of cobalt and copper ions, which were found to also bind with a molar ratio of 2 to the three 5′-nucleotidases tested. © 1990.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
