Studies on the heparin sulphamidase activity from rat spleen. Intracellular distribution and characterization of the enzyme.
A sulphamidase activity present in rat spleen capable of hydrolysing N-[(35)S]sulphated heparin was studied. This activity was associated with the lysosomal fraction. Studies in vivo showed that the rat is capable of significantly desulphating heparin. Lysosomes in all the major tissues can effectively accumulate heparin. The heparin sulphamidase and arylsulphatase activities from rat spleen were separated by isoelectric focusing. Heparin sulphamidase was a distinct entity from all the arylsulphatase activities.
D000818:Animals; D002499:Centrifugation, Density Gradient; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006493:Heparin; D006867:Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D007700:Kinetics; D008247:Lysosomes / Q000032:analysis / Q000378:metabolism; D008928:Mitochondria; D008970:Molecular Weight; D051381:Rats; D013053:Spectrophotometry; D013154:Spleen / Q000201:enzymology*; D013347:Subcellular Fractions; D013429:Sulfatases; D013462:Sulfur Radioisotopes
D013462:Sulfur Radioisotopes; D006493:Heparin; D006867:Hydrolases; D013429:Sulfatases; C022708:N-sulfoglucosamine sulfohydrolase