We investigated the synthesis and accumulation of vegetative storage proteins (VSPs) in poplar plantlets and the homology between poplar seed storage proteins (SSPs) and VSPs. One-dimensional SDS polyacrylamide gel electrophoresis confirmed that both seed and vegetative storage proteins contained two predominant polypeptides of MW 32 and 36 kDa, but the subunit composition of the polypeptides differed. The 32- and 36-kDa polypeptides were highly abundant in basal leaves, stems, and roots of poplar plantlets. The 36-kDa subunit was synthesized in all plantlet tissues examined, but the 32-kDa subunit was not, suggesting that the 36-kDa polypeptide is a precursor of the 32-kDa polypeptide. The 36- and 32-kDa polypeptides of both SSPs and VSPs were glycosylated and both were found to be albumins. In addition, both polypeptides cross-reacted with a VSP antibody. Protein fingerprint patterns generated with two different proteolytic enzymes were identical for the 36-kDa polypeptide isolated from seeds or from stem tissue. Our study provides evidence that poplar SSPs and VSPs exhibit homology, and that expression is neither tissue-specific nor regulated solely by photoperiod.