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The acid hydrolase GUSB (s-D-glucuronoside glucuronosohydrolase, E.C. 3.2.1.31) plays an essential role in catabolism of glucuronic acid containing glycosaminoglycans (GAGs). It cleaves s-glucuronosyl residues at the non-reducing end of oligosaccharides from GAGs. GUSB degrades sulphated glycosaminoglycans such as heparan, dermatan and chondroitin and is involved in the catabolic pathway of hyaluronic acid. GUSB deficiency causes the lysosomal storage disorder Mucopolysaccharidosis type VII. Clinical and biochemical findings of MPSVII in human were first described by Sly et al. (1973). Fyfe et al. (1999) reported a G→A transition at position 1074 of an MPSVII affected cat GUSB cDNA. GUSB is already assigned to human chromosome 7q21.11. Here we report the localization of the porcine GUSB gene to chromosome SSC3p16→p14 by FISH and confirm the position by screening of hybrid panels.

Assignment of the β-glucuronidase (GUSB) gene to porcine chromosome SSC3p16→p14 by FISH and confirmation by hybrid panel analyses