Two cell-surface proteins were identtjied in the dinoflagellate Prorocentrum minimum (Pavillard) Schilkr strain CCMP 1329 that are evident in phosphate-limited cultures, but not in nitrate-limited cultures or cultures growing exponentially in complete media. These proteins were detected by labeling cell-surface proteins with the biotinylating reagent succinimidyl d(biotinamid0) hexanoate. One protein, of appoximately 200,000 daltons was purfied using dqferential centrifugation, detergent extraction, and gel filtration chromatography. This purif;ed protein was able to hydrolyu orthophosphate groups from pnitrophenyl$hosphate at PH 8, indicating it is an alkaline phosphatase, although it is larger than other alkaline phosphatases isolated to date t o m most microorganisms. This potein may be induced to help P. minimum cleave orthophosphate groups from organic forms of phosphate in marine environments. Ultimately, this potein could represent a unique antigen for developing an antibody pobe for examining the relationships between phosphate stress and bloom formation in P. minimum, and perhaps other dinojagellates, in the field.