Polyamine-peptide conjugates: proposed functions
Rennert, O.M.; Chan, W.Y.; Griesmann, G.
Physiological Chemistry and Physics 12(5): 441-450
1980
ISSN/ISBN: 0031-9325 PMID: 7208640 Document Number: 154685
Six polyamine-conjugated proteins were identified in human amniotic fluid. Three contained covalently bound spermine, one contained covalently bound spermidine, and two contained covalently bound putrescine. All were characterized by high content of serine, glycine, glutamate, and aspartate. Polyamination of proteins may participate in mechanisms for (1) polyamine specificity in cell growth; (2) cell surface attachment of polyamines; (3) transport of polyamines; (4) endocytosis and other cellular uptake processes; and (5) signaling protein degradation.