Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. Galactoside-binding soluble lectin 13 has lysophospholipase activity. It is composed of two identical subunits which are held together by disulfide bonds. This protein has structural similarity to several members of the beta-galactoside-binding S-type lectin family.By ultracentrifugation and SDS-PAGE, LGALS13 showed an apparent molecular mass of 29 to 30 kD.

Under reducing conditions, the apparent molecular mass was 16 kD, suggesting that LGALS13 is composed of 2 identical subunits held together by disulfide bonds. Western blot analysis and Ouchterlony gel diffusion were unable to detect LGALS13 in serum or in any other adult or fetal tissue examined.