The objective of this research is to partially characterize proteins extracted from Terminalia catappa seeds that behave like lectin, being capable of mouse sperm agglutination. Cotyledons of the seed were extracted in homogenizing PBS buffer. The supernatant was precipitated with ammonium sulfate to a final concentration of 50% (w/v), then dialyzed with 2 kinds of dialysis tubes, i.e. 6000 and 12000 MWCO. The precipitated proteins were then diluted in 0.9% (w/v) NaCl. Next, dialysis fractions of the precipitated protein were used for the mouse sperm agglutination test. Protein from the dialysis fraction of 6000 MWCO tube could agglutinate mouse sperm. The quantitation of protein was carried out by using the Bradford Coomassie kit from crude extract to dialyzed fractions. Both dialyzed fractions were also run on SDS-PAGE to see the protein profiles.

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