Arabinogalactan-proteins (AGPs) have been purified from the plasma membrane of suspension-cultured Paul's Scarlet rose (Rosa sp.) cells. The two most abundant and homogeneous plasma membrane ACP fractions were named plasma membrane ACPl (PM-ACP1) and plasma membrane AGP2 (PM-ACP2) and had apparent molecular masses of 140 and 21 7 kD, respectively. Both PM-ACP1 and PM-ACP2 had p-(l-3)-, p-(1,6)-, and p-(1,3,6)-galactopyranosyl residues, predominantly terminal a-arabinofuranosyl residues, and (1,4)-and terminal glucuronopyranosyl residues. The protein moieties of PM-ACP1 and PM-ACP2 were both rich in hydroxyprolhe, alanine, and serine, but differed in the abundance of hydroxyproline, which was 1.6 times higher in PM-ACP2 than in PM-ACP1. Another difference was the overall protein content, which was 3.7% (w/w) in PM-ACP1 and 15% in PM-ACP2. As judged by their behavior on reverse-phase chromatography, PMACPl and PM-ACP2 were not more hydrophobic than ACPs from the cell wall or culture medium. In contrast, a minor plasma membrane ACP fraction eluted later on reverse-phase chromatography and was more negatively charged at pH 5 than either PM-ACP1 or PM-ACP2. The more negatively charged fraction contained molecules with a glycosyl composition characteristic of ACPs and included at least two different macromolecules. The results of this investigation indicate that Rosa plasma membrane contains at least four distinct ACPs or ACP-like molecules. These molecules differed from each other in size, charge, hydrophobicity, amino-acyl composition, and/or protein content.AGPs are a class of proteoglycans that are rich in galactosyl and arabinosyl residues Fincher et al., 1983; Bacic et al., 1988), and they appear to be present in all plant cells (Jermyn and Yeow, 1975;