Expression of human gelatinase B in Pichia pastoris

Full-length human gelatinase B (FLGelB) and its C-terminal truncated form ( dGelB) were expressed in Pichia pastoris strain GS115, using the Saccharomy ces cerevisiae Mat alpha signal peptide. In both cases, a high level of the secreted protein could be detected by SDS-PAGE. The truncated gene was als o expressed using the human gelatinase B native signal peptide, Secretion u sing the Mat alpha signal peptide was significantly greater than that from the native signal peptide. The recombinant products were purified and chara cterized biochemically. The recombinant proteins, FLGelB and dGelB, were fo und to have similar biochemical properties and activity to that of the huma n gelatinase B native protein. (C) 1999 Academic Press.