Major polypeptide species of proteins have been identified and analysed by sodium dodecyl sulphate polyacrylamide gel electrophoresis in fresh extracts of the whole leaf, leaf gel, root and stalk portions of Aloe barbudensis Miller plants of immature, young and mature ages. Extracts of the fresh Aloe plant portions were prepared by dissection, tissue disruption, differential centrifugation and gel filtration methods. Extracted plant portions analysed by separation electrophoresis were also assayed by biochemical and immunological techniques for the presence of lectin associated reactions, i.e. agglutination or mitogenicity. Results of the separation electrophoresis analysis of extracts prepared from fresh whole leaves and leaf gel of mature Aloe barbadensis Miller plants revealed 23 identifiable difterent polypeptides. Molecular weights of these polypeptides, calculated from sets of molecular weight reference standards, ranged from 70000 for the largest to 3OOO for the smallest. Electrophoresis profiles of commercially processed and freshly processed Aloe barbadensis Miller and Aloe suponaria Haw leaf gel extracts revealed similar patterns for major peptides. Treatment of mature whole Aloe leaf extracts with acidic and alkaline conditions revealed distinct changes in pH stability of ten peptides. Comparisons of separation electrophoresis profiles of fresh extracts of Aloe whole leaves and of leaf gel portions revealed marked differences in both molecular weights and concentrations of peptides found in extracts from mature, young or immature plants. This report is the first to describe the nature and types of polypeptides detected in extracts of whole leaf, leaf gel, stalk and root portions of immature, young and mature Aloe plants. Accordingly, information in this report may be of considerable value in helping to identify and characterize Aloe substances present during processing in extracts and in products.