Guncar, G <br/><br/>
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function.  [electronic resource] 

 -  Structure (London, England : 1993)  Jan 1998 
 - 51-61 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0969-2126 
<br/><br/><label>Standard No.: </label>10.1016/s0969-2126(98)00007-0  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Aminopeptidases--chemistry<br/>Animals<br/>Binding Sites--physiology<br/>Cathepsin B--chemistry<br/>Cathepsin H<br/>Cathepsins--chemistry<br/>Crystallography, X-Ray<br/>Cysteine Endopeptidases--chemistry<br/>Cysteine Proteinase Inhibitors--metabolism<br/>Glycosylation<br/>Lysosomes--enzymology<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Oligosaccharides--chemistry<br/>Protein Precursors--chemistry<br/>Protein Processing, Post-Translational--physiology<br/>Protein Structure, Secondary<br/>Sequence Alignment<br/>Swine