scholarly journals Rapid purification and characterization of protein kinase C from bovine retinal rod outer segments

1991 ◽  
Vol 201 (3) ◽  
pp. 601-606 ◽  
Author(s):  
Gregor WOLBRING ◽  
Neil J. COOK
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rod Outer Segments ◽  
Purification And Characterization ◽  
Outer Segments ◽  
Kinase C ◽  
Retinal Rod ◽  
Rapid Purification ◽  
Retinal Rod Outer Segments

Purification and Characterization of Protein Kinase C from a Higher Plant, Brassica campestris L

1994 ◽  
Vol 203 (1) ◽  
pp. 311-318 ◽  
Author(s):  
T. Nanmori ◽  
W. Taguchi ◽  
M. Kinugasa ◽  
Y. Oji ◽  
S. Sahara ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Brassica Campestris ◽  
Purification And Characterization ◽  
Higher Plant ◽  
Kinase C

scholarly journals Protein kinase C in rod outer segments: effects of phosphorylation of the phosphodiesterase inhibitory subunit

1996 ◽  
Vol 317 (1) ◽  
pp. 291-295 ◽  
Author(s):  
Igor P. UDOVICHENKO ◽  
Jess CUNNICK ◽  
Karen GONZALEZ ◽  
Alexander YAKHNIN ◽  
Dolores J. TAKEMOTO
Keyword(s):  
Protein Kinase C ◽  
Catalytic Activity ◽  
Protein Kinase ◽  
Direct Interaction ◽  
Inhibitory Effect ◽  
Rod Outer Segments ◽  
Visual Transduction ◽  
Gtp Hydrolysis ◽  
Outer Segments ◽  
Kinase C

The inhibitory subunit (PDEγ) of the cGMP phosphodiesterase (PDEαβγ2) in rod outer segments (ROS) realizes its regulatory role in phototransduction by inhibition of PDEαβ catalytic activity. The photoreceptor G-protein, transducin, serves as a transducer from the receptor (rhodopsin) to the effector (PDE) and eliminates the inhibitory effect of PDEγ by direct interaction with PDEγ. Our previous study [Udovichenko, Cunnick, Gonzalez and Takemoto (1994) J. Biol. Chem. 269, 9850–9856] has shown that PDEγ is a substrate for protein kinase C (PKC) from ROS and that phosphorylation by PKC increases the ability of PDEγ to inhibit PDEαβ catalytic activity. Here we report that transducin is less effective in activation of PDEαβ(γp)2 (a complex of PDEαβ with phosphorylated PDEγ, PDEγp) than PDEαβγ2. PDEγp also increases the rate constant of GTP hydrolysis of transducin (from 0.16 s-1 for non-phosphorylated PDEγ to 0.21 s-1 for PDEγp). These data suggest that phosphorylation of the inhibitory subunit of PDE by PKC may regulate the visual transduction cascade by decreasing the photoresponse.

scholarly journals Purification and characterization of Ca2+phospholipid dependent protein kinase (C kinase) from human platelets.

1985 ◽  
Vol 16 (6) ◽  
pp. 614-617
Author(s):  
Masakatsu NISHIKAWA ◽  
Hiroyoshi HIDAKA ◽  
Shigeru SHIRAKAWA ◽  
Robert S. ADELSTEIN
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Human Platelets ◽  
Purification And Characterization ◽  
Dependent Protein Kinase ◽  
Kinase C ◽  
Dependent Protein
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