Yasuda, Y <br/><br/>
Evidence for the presence of two kinetically distinct active forms of ribonuclease T2. The pH dependence of the steady-state kinetic parameter, kcat, for transphosphorylation of both a natural and a synthetic substrate.  [electronic resource] 

 -  European journal of biochemistry  Feb 1981 
 - 229-34 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0014-2956 
<br/><br/><label>Standard No.: </label>10.1111/j.1432-1033.1981.tb05140.x  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Binding Sites<br/>Buffers<br/>Endonucleases--metabolism<br/>Endoribonucleases<br/>Hydrogen-Ion Concentration<br/>Isoenzymes--metabolism<br/>Kinetics<br/>Protein Binding<br/>Ribonucleases--metabolism<br/>Substrate Specificity