Maccarrone, M <br/><br/>
Tryptic digestion of soybean lipoxygenase-1 generates a 60 kDa fragment with improved activity and membrane binding ability.  [electronic resource] 

 -  Biochemistry  Jun 2001 
 - 6819-27 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi010187m  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Binding Sites<br/>Circular Dichroism<br/>Enzyme Activation<br/>Hydrolysis<br/>Kinetics<br/>Liposomes--metabolism<br/>Lipoxygenase--chemistry<br/>Membrane Proteins--chemistry<br/>Molecular Weight<br/>Peptide Fragments--chemistry<br/>Protein Binding<br/>Glycine max--enzymology<br/>Spectrometry, Fluorescence<br/>Spectrophotometry, Ultraviolet<br/>Substrate Specificity<br/>Trypsin--metabolism