Yang, G <br/><br/>
Steady-state kinetic characterization of substrates and metal-ion specificities of the full-length and N-terminally truncated recombinant human methionine aminopeptidases (type 2).  [electronic resource] 

 -  Biochemistry  Sep 2001 
 - 10645-54 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi010806r  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Substitution<br/>Aminopeptidases--antagonists & inhibitors<br/>Anilides<br/>Cations, Divalent<br/>Circular Dichroism<br/>Humans<br/>Isoenzymes--genetics<br/>Kinetics<br/>Metalloendopeptidases--antagonists & inhibitors<br/>Metals--metabolism<br/>Norleucine--analogs & derivatives<br/>Recombinant Proteins--genetics<br/>Spectrophotometry<br/>Substrate Specificity