Cantor, A B <br/><br/>
Lysosomal enzyme phosphorylation. II. Protein recognition determinants in either lobe of procathepsin D are sufficient for phosphorylation of both the amino and carboxyl lobe oligosaccharides.  [electronic resource] 

 -  The Journal of biological chemistry  Nov 1992 
 - 23349-56 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Animals<br/>Base Sequence<br/>Binding Sites<br/>Carbohydrate Conformation<br/>Carbohydrate Sequence<br/>Cathepsin D--genetics<br/>Chromatography, Affinity<br/>Chromatography, Ion Exchange<br/>Cloning, Molecular<br/>Enzyme Precursors--genetics<br/>Female<br/>Glycopeptides--biosynthesis<br/>Humans<br/>Kidney--enzymology<br/>Lysosomes--enzymology<br/>Mannose--metabolism<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Oligodeoxyribonucleotides<br/>Oligosaccharides--metabolism<br/>Pepsinogens--genetics<br/>Phosphorylation<br/>Phosphotransferases--metabolism<br/>Plasmids<br/>Polymerase Chain Reaction<br/>Protein Conformation<br/>Transferases (Other Substituted Phosphate Groups)<br/>Xenopus laevis