The poor stability of crude solutions of fusicoccin-binding sites, prepared from acetonedried microsomal fractions of spinach leaves, results from the attack by endogenous phosphatase and -mannosidase. The addition of either of these enzymes to solubilised binding sites preincubated with [3H]fusicoccin promptly releases most of the bound radioactivity. A satisfactory stabilization of the crude preparations is obtained with fluoride added either during homogenization of the tissue, or immediately after solubilisation. The results indicate that the fusicoccin-binding sites are phosphorylated glycoproteins.
Aducci, P., Ballio, A., Fiorucci, L., Simonetti, E. (1984). Inactivation of solubilised fusicoccin-binding sites by endogenous plant hydrolases. PLANTA, 160(5), 422-427 [10.1007/BF00429758].
Inactivation of solubilised fusicoccin-binding sites by endogenous plant hydrolases
ADUCCI, PATRIZIA;FIORUCCI, LAURA;
1984-01-01
Abstract
The poor stability of crude solutions of fusicoccin-binding sites, prepared from acetonedried microsomal fractions of spinach leaves, results from the attack by endogenous phosphatase and -mannosidase. The addition of either of these enzymes to solubilised binding sites preincubated with [3H]fusicoccin promptly releases most of the bound radioactivity. A satisfactory stabilization of the crude preparations is obtained with fluoride added either during homogenization of the tissue, or immediately after solubilisation. The results indicate that the fusicoccin-binding sites are phosphorylated glycoproteins.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.