ABSTRACT
α-Galactosidase, a lysosomal enzyme, is a part of the degradation pathway for glycolipids that is involved in the sequential removal of the glycans, leaving behind the core lipid, ceramide. Human α-galactosidase is a noncovalently-linked homodimeric glycoprotein with molecular mass of approximately 100 kDa. The nutritive value of soybean meal can be improved by treatment with α-galactosidase. Although human α-galactosidase has been crystallized, only a preliminary X-ray analysis has been made and no structure has been published yet. The human a-galactosyl hydrolase α-GAL gene was isolated, spliced into a bacterial plasmid, and then inserted into the Chinese hamster ovary cell. Preclinical studies of the active ingredient in Fabrazyme were performed in several animal models, including α-GAL knockout mouse. The purified α-GAL is stabilized with excipients and undergoes double-sterile filtration before it is distributed into vials under aseptic conditions. The vials are lyophilized in either 20 cc or 5 cc configurations to enhance stability and storage.
