Analysis of affinity-purified preparations of the fetuin-binding prote
ins from elderberry bark and fruits revealed besides the previously re
ported Neu5Ac(alpha-2,6)Gal/GalNAc-specific type 2 ribosome-inactivati
ng proteins (RIP) the occurrence of single chain proteins of 22 kDa, w
hich according to their N-terminal a!nino acid sequence correspond to
the second part of the B chain of the respective type 2 RIP, Both prot
eins are very similar except that the polypeptides of the fruit lectin
are 10 amino acid residues longer than these from the bark lectin, Ou
r findings not only demonstrate the occurrence of carbohydrate-binding
fragments of type :! RIP but also provide further evidence that type
2 RIP genes give rise to complex mixtures of type 2 RIP/lectins in eld
erberry. (C) 1998 Federation of European Biochemical Societies.