title: Inactivation of solubilised fusicoccin-binding sites by endogenous plant hydrolases.
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 α-mannosidase. The addition of either of these enzymes to solubilised binding sites preincubated with [(3)H]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.
authors.affiliation: Gruppo di Chimica Biologica e Strutturistica Chimica della Facoltà di Scienze, Università di Roma "La Sapienza", Città Universitaria, I-00185, Rome, Italy.
authors.forename: P
authors.initials: P
authors.lastname: Aducci
authors.forename: A
authors.initials: A
authors.lastname: Ballio
authors.forename: L
authors.initials: L
authors.lastname: Fiorucci
authors.forename: E
authors.initials: E
authors.lastname: Simonetti