Ricin-binding properties of acid hydrolases from isolated lysosomes implies prior processing by terminal transferases of the trans-Golgi apparatus |
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Authors: | K N Fedde W S Sly |
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Institution: | 1. Catalonian Antidoping Laboratory, IMIM, Hospital del Mar Medical Research Institute, Barcelona, Spain;2. Pompeu Fabra University, Barcelona, Spain;1. ,;2. Sanofi R&D, Montpellier, France;3. Sanofi R&D, Marcy l''Etoile, France |
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Abstract: | Acid hydrolases were isolated from the lysosome fraction of beta-galactosidase-deficient human fibroblasts and from the mannose 6-phosphate containing medium in which they were grown. Nearly half of the total beta-hexosaminidase and beta-glucuronidase from both sources bound to Ricin specifically. Lysosomal beta-hexosaminidase, metabolically labelled with 35S]-methionine, was also fractionated on Ricin-agarose. SDS-PAGE of immunoprecipitates from Ricin-binding and non-binding fractions revealed approximately equivalent amounts of cross-reacting material at the appropriate MW. We interpret these results to mean that acid hydrolases which are segregated to lysosomes are exposed to trans-Golgi processing enzymes to about the same extent as enzymes which are secreted, and that segregation by the Man 6-P receptor occurs after transit through the trans-Golgi compartment. |
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