The Effects of the Site-Directed Removal of N-Glycosylation from Cationic Peanut Peroxidase on Its Function

2001 ◽  
Vol 386 (1) ◽  
pp. 17-24 ◽  
Author(s):  
Bao Lige ◽  
Shengwu Ma ◽  
Robert B. van Huystee
Keyword(s):  
Plant Science ◽  
1998 ◽  
Vol 136 (2) ◽  
pp. 159-168 ◽  
Author(s):  
Bao Lige ◽  
Shengwu Ma ◽  
Dongling Zhao ◽  
Robert B. van Huystee

1997 ◽  
Vol 45 (11) ◽  
pp. 4196-4200 ◽  
Author(s):  
Yan Sun ◽  
Bao Lige ◽  
Robert B. van Huystee

1984 ◽  
Vol 62 (11) ◽  
pp. 1046-1050 ◽  
Author(s):  
R. N. Chibbar ◽  
R. Cella ◽  
R. B. Van Huystee

Heme is present in an equimolar ratio to the apoprotein in the major cationic fraction of peanut peroxidase. The removal of heme from the holoenzyme does not affect the physicochemical and immunological properties of the apoperoxidase, however peroxidase activity is completely lost. The indoleacetic acid (IAA) oxidase activity of the apoperoxidase is reduced to 1/20 of the original holoenzyme. Both the peroxidase and IAA-oxidase activity could partially be restored in the holoenzyme reconstituted with hemin. It is suggested that heme may also participate in the IAA-oxidase activity possibly by altering the active site.


1984 ◽  
Vol 116 (4) ◽  
pp. 365-373 ◽  
Author(s):  
Ravindra N. Chibbar ◽  
Robert B. Van Huystee
Keyword(s):  

2005 ◽  
Vol 66 (16) ◽  
pp. 1869-1879 ◽  
Author(s):  
Ranjith Pathirana ◽  
Lyn Watson ◽  
Balance Chen ◽  
Susanna Leung ◽  
Christine Voisey ◽  
...  

1977 ◽  
Vol 16 (11) ◽  
pp. 1657-1659 ◽  
Author(s):  
Om.P. Srivastava ◽  
R.B. van Huystee

1987 ◽  
Vol 85 (1) ◽  
pp. 299-303 ◽  
Author(s):  
Chunfang Hu ◽  
Daniela Carbonera ◽  
Robert van Huystee

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