The characterization of macromolecules from shell matrix proteins in living organisms is the fundamental first step in establishing molecular phylogenies. This is particularly important if ancient macromolecules will be used for the phylogenies. Approximately 500 individuals of Orbulina universa were picked from plankton tows taken in the Gulf of Mexico during spring 1990. Proteins were extracted from the tests of the individuals, and the molecular weights of the proteins were determined and compared to 2,000–4,000-year old samples. Gel electrophoresis of the soluble matrix (SM) from living O. universa showed at least ten protein bands, while electrophoresis of core-top O. universa showed two protein bands. Dot-immunobinding assays of proteins from living and fossil samples of O. universa, incubated against monoclonal antibodies raised against core-top O. universa SM, demonstrated a reactivity with the two proteins in common. Less reactivity was obtained with living samples of the benthic foraminifers Androsina lucasi and Archaias angulatus and core-top samples of the planktonic foraminifer Neogloboquadrina dutertrei. A partial protein sequence from one shell matrix protein approximately 65kD in size, from core-top Orbulina universa, showed a domain of polyaspartic acid at the NH2 terminus. This is consistent with data obtained for other matrix proteins found in invertebrates and vertebrates. Sequence data provide insight into the role that the protein may play in the biomineralization of the test and will aid in modelling degradation. □Foraminifera, test proteins, monoclonal antibodies, Orbulina, Androsina, Archaias, Neogloboquadrina, biomineralization, Dot-immunobinding assay, protein sequence.