Selective isolation, purification, secondary structure and functional properties of some globulins of Chia (Salvia hispanica L.) were studied. These globulins were isolated using water and two different NaCl concentrations (5 and 10%) and testing four enzymatic assays: polyphenol oxidase, catalase, peroxidase and chymoprotease for each extraction. Maximum protein extraction (18.4%) and highest enzymatic activity occurred in the presence of 5% NaCl. The main globulin protein was obtain using gel filtration chromatography and shows an increase of polyphenol oxidase, chymoprotease and proteolytic activities; and a decrease of catalase activity as compared with the crude extract. Further purification using anion-exchange chromatography produces two globulins SB1Q2 and SB1Q3 with molecular weights of 10 and 13 kDa and isoelectric points of 4.5 and 6.8, respectively. Their secondary structure using circular dichroism showed 42, 7%; 42.1, 7.4% of β-sheet and helical structures, respectively. This observation agrees well with the secondary structure of globulins in plant dicotyledonous seeds.