scholarly journals Purification and Partial Characterization of Two Acidic Proteases from the White-Rot Fungus Sporotrichum pulverulentum

2005 ◽  
Vol 124 (3) ◽  
pp. 635-642 ◽  
Author(s):  
Karl-Erik ERIKSSON ◽  
Bert PETTERSSON
1986 ◽  
Vol 236 (1) ◽  
pp. 221-226 ◽  
Author(s):  
F F Morpeth ◽  
G D Jones

Four forms of cellobiose quinone dehydrogenase have been purified from the white-rot fungus Sporotrichum pulverulentum. The Mr of the enzyme has been estimated by sedimentation equilibrium to be 57,800 and by SDS/polyacrylamide-gel to be 60,000. These enzymes are clearly monomers. Cellobiose quinone dehydrogenases contain FAD and variable amounts of a green chromophore which we suggest is 6-hydroxy-FAD. The superoxide anion and H2O2 are the products of its reaction with oxygen. All of the isoenzymes from any one preparation display similar kinetic parameters. However, these vary between preparations. The only apparent difference between the four separable isoenzymes is their neutral-sugar content.


2015 ◽  
Vol 25 (1) ◽  
pp. 57-65 ◽  
Author(s):  
Julieta Mallerman ◽  
Leandro Papinutti ◽  
Laura Levin

2019 ◽  
Vol 66 (4) ◽  
pp. 131-137
Author(s):  
Sangho Koh ◽  
Seika Imamura ◽  
Naoto Fujino ◽  
Masahiro Mizuno ◽  
Nobuaki Sato ◽  
...  

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