Mäkinen, P L <br/><br/>
An endo-acting proline-specific oligopeptidase from Treponema denticola ATCC 35405: evidence of hydrolysis of human bioactive peptides.  [electronic resource] 

 -  Infection and immunity  Nov 1994 
 - 4938-47 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0019-9567 
<br/><br/><label>Standard No.: </label>10.1128/iai.62.11.4938-4947.1994  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Amino Acids--analysis<br/>Angiotensin II--metabolism<br/>Bradykinin--metabolism<br/>Chelating Agents--pharmacology<br/>Enzyme Activation--drug effects<br/>Histidine<br/>Humans<br/>Hydrogen-Ion Concentration<br/>Kinetics<br/>Molecular Sequence Data<br/>Molecular Weight<br/>Oligopeptides--metabolism<br/>Prolyl Oligopeptidases<br/>Sequence Alignment<br/>Sequence Homology, Amino Acid<br/>Serine<br/>Serine Endopeptidases--chemistry<br/>Sodium Chloride--pharmacology<br/>Structure-Activity Relationship<br/>Substance P--metabolism<br/>Substrate Specificity<br/>Sulfhydryl Compounds--pharmacology<br/>Temperature<br/>Treponema--enzymology<br/>Vasopressins--metabolism