scholarly journals A Second Extensin-Like Hydroxyproline-Rich Glycoprotein from Carrot Cell Walls

1987 ◽  
Vol 84 (3) ◽  
pp. 820-825 ◽  
Author(s):  
Joel P. Stafstrom ◽  
L. Andrew Staehelin
Keyword(s):  
1986 ◽  
Vol 81 (1) ◽  
pp. 234-241 ◽  
Author(s):  
Joel P. Stafstrom ◽  
L. Andrew Staehelin
Keyword(s):  

2008 ◽  
Vol 56 (18) ◽  
pp. 8558-8564 ◽  
Author(s):  
Yoon-Han Kang ◽  
Charlotte C. Parker ◽  
Andrew C. Smith ◽  
Keith W. Waldron
Keyword(s):  

1976 ◽  
Vol 18 (2) ◽  
pp. 263-269 ◽  
Author(s):  
D. Dudits ◽  
K. N. Kao ◽  
F. Constabel ◽  
O. L. Gamborg

Fusion of protoplasts from cultured cells of carrot (Daucus carota L.) and from leaves of barley (Hordeum vulgare L.) by means of polyethylene glycol resulted in the formation of 4-5 fusion products (heterokaryocytes) per 100 protoplasts. When incubated in culture medium, the heterokaryocytes regenerated cell walls and divided. The frequency of division depended on the viability of the protoplasts from carrot cell cultures, specifically, on the mitotic activity of the cells. Fusion of interphase carrot and barley nuclei was detected by differential staining. Synchronized mitosis was observed in heterokaryons containing barley and carrot nuclei.


1976 ◽  
Vol 15 (1) ◽  
pp. 165-169 ◽  
Author(s):  
Cho Yong-Pill ◽  
Maarten J. Chrispeels
Keyword(s):  

1997 ◽  
Vol 45 (7) ◽  
pp. 2468-2471 ◽  
Author(s):  
Adrian J. Parr ◽  
Annie Ng ◽  
Keith W. Waldron

2015 ◽  
Vol 43 ◽  
pp. 41-50 ◽  
Author(s):  
Justyna Cybulska ◽  
Artur Zdunek ◽  
Arkadiusz Kozioł

1970 ◽  
Vol 18 (5) ◽  
pp. 878-880 ◽  
Author(s):  
Ronald J. Echandi ◽  
Betty R. Chase ◽  
Louis M. Massey

2014 ◽  
Vol 8 (1) ◽  
pp. 171-180 ◽  
Author(s):  
Joanna Mierczyńska ◽  
Justyna Cybulska ◽  
Piotr M. Pieczywek ◽  
Artur Zdunek
Keyword(s):  

2004 ◽  
Vol 379 (3) ◽  
pp. 601-607 ◽  
Author(s):  
Benoît van der REST ◽  
Norbert ROLLAND ◽  
Anne-Marie BOISSON ◽  
Myriam FERRO ◽  
Richard BLIGNY ◽  
...  

GPX-PDE (glycerophosphodiester phosphodiesterase; EC 3.1.4.46) is a relatively poorly characterized enzyme that catalyses the hydrolysis of various glycerophosphodiesters (glycerophosphocholine, glycerophosphoethanolamine, glycerophosphoglycerol, glycerophosphoserine and bis-glycerophosphoglycerol), releasing sn-glycerol 3-phosphate and the corresponding alcohol. In a previous study, we demonstrated the existence of a novel GPX-PDE in the cell walls and vacuoles of plant cells. Since no GPX-PDE had been identified in any plant organism, the purification of GPX-PDE from carrot cell walls was attempted. After extraction of cell wall proteins from carrot cell suspension cultures with CaCl2, GPX-PDE was purified up to 2700-fold using, successively, ammonium sulphate precipitation, gel filtration and concanavalin A–Sepharose. Internal sequence analysis of a 55 kDa protein identified in the extract following 2700-fold purification revealed strong similarity to the primary sequence of GLPQ, a bacterial GPX-PDE. To confirm the identity of plant GPX-PDE, an Arabidopsis thaliana cDNA similar to that encoding the bacterial GPX-PDE was cloned and overexpressed in a bacterial expression system, and was used to raise antibodies against the putative Arabidopsis thaliana GPX-PDE. Immunochemical assays performed on carrot cell wall proteins extracted by CaCl2 treatment showed a strong correlation between GPX-PDE activity and detection of the 55 kDa protein, validating the identity of the plant GPX-PDE. Finally, various properties of the purified enzyme were investigated. GPX-PDE is a multimeric enzyme, specific for glycerophosphodiesters, exhibiting a Km of 36 µM for glycerophosphocholine and active within a wide pH range (from 4 to 10). Since these properties are similar to those of GLPQ, the bacterial GPX-PDE, the similarities between plant and bacterial enzymes are also discussed.


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