As a basic work of illustrating the relationship between the structure and function of a kind of protein purified from Se-enriched Ganoderma lucidum (Se-GL-P), the primary biochemical characters of Se-GL-P were characterized. Molecular mass was determined by two methods of sodium dodecyl sulfate polyacrylamide gel electrophoresis and size exclusion chromatogram. Amino acids composition, isoelectric point, peptide mass fingerprint, and the sequence of N terminal amino acids were determined by high performance liquid chromatography, capillary isoelectric focusing method, in-gel digestion, and Edman digestion method respectively. Results showed that, the Mr of Se-GL-P was 36 600, pI = 4.01, and the sequence of N-terminal amino acids was DINGGGATLPQKLYLTPDVL. A conclusion was drawn that Se-GL-P was a kind of new selenium-containing protein, and it was one member of DING protein family.