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dc.contributor.supervisor Dr. Barbara Triggs-Raine (Biochem. and Med. Genetics) Dr. Steve Pind (Biochem. and Med. Genetics) en
dc.contributor.author Patel, Nehal
dc.date.accessioned 2006-04-04T15:30:16Z
dc.date.available 2006-04-04T15:30:16Z
dc.date.issued 2006-04-04T15:30:16Z
dc.identifier.uri http://hdl.handle.net/1993/233
dc.description.abstract Hyaluronidases are endoglycosidases that catabolize hyaluronan, an abundant component of the extracellular matrix surrounding vertebrate cells. We characterized one of the hyaluronidases, HYAL1, an enzyme deficient in the lysosomal storage disorder Mucopolysaccharidosis IX. HYAL1 stably expressed in BHK cells resulted in several intracellular forms, but only one secreted form. Secretion was not increased by weak bases, and no phosphate was incorporated in metabolic labeling, suggesting this enzyme is not targeted to the lysosome by the mannose 6-phosphate dependent pathway. Further analysis revealed the various forms of HYAL1 differ only in glycosylation, and are all active at pH 3.8. The forms migrated in a Percol density gradient similarly to an endosomal marker, and with partial overlap with the lysosomal marker LPG120 (Lamp1). en
dc.format.extent 4985394 bytes
dc.format.mimetype application/pdf
dc.language.iso en_US
dc.rights info:eu-repo/semantics/openAccess
dc.subject Hyaluronan en
dc.subject Hyal1
dc.title The subcellular localization and targeting pathway of hyaluronidase1 en
dc.type info:eu-repo/semantics/masterThesis
dc.type master thesis en_US
dc.degree.discipline Biochemistry & Medical Genetics en
dc.contributor.examiningcommittee Dr. Gilbert Arthur (Biochemistry and Medical Genetics) Dr. John Wilkins (Internal medicine/Immunology) en
dc.degree.level Master of Science (M.Sc.) en
dc.description.note May 2006 en


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