Partial purification and characterization of the soluble DNA polymerase (polymerase-?) from seedlings of Pisum sativum L.

Planta ◽  
1978 ◽  
Vol 138 (2) ◽  
pp. 127-132 ◽  
Author(s):  
Christine Stevens ◽  
John A. Bryant
Keyword(s):  
Pisum Sativum ◽  
Dna Polymerase ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Pisum Sativum L

Partial purification and characterization of mitochondrial DNA polymerase from Plasmodium falciparum

2000 ◽  
Vol 49 (4) ◽  
pp. 279-288 ◽  
Author(s):  
Porntip Chavalitshewinkoon-Petmitr ◽  
Srisucha Chawprom ◽  
Lieve Naesens ◽  
Jan Balzarini ◽  
Prapon Wilairat
Keyword(s):  
Plasmodium Falciparum ◽  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Partial Purification ◽  
Purification And Characterization ◽  
Mitochondrial Dna Polymerase

Partial purification and characterization of the DNA polymerase from the cyanelles of Cyanophora paradoxa

FEBS Letters ◽  
1997 ◽  
Vol 410 (2-3) ◽  
pp. 509-514 ◽  
Author(s):  
Melissa A White ◽  
J.Clinton Bailey II ◽  
Gordon C Cannon ◽  
Sabine Heinhorst
Keyword(s):  
Dna Polymerase ◽  
Partial Purification ◽  
Cyanophora Paradoxa ◽  
Purification And Characterization

scholarly journals The purification and characterization of a third storage protein (convicilin) from the seeds of pea (Pisum sativum L.)

1980 ◽  
Vol 191 (2) ◽  
pp. 509-516 ◽  
Author(s):  
R R Croy ◽  
J A Gatehouse ◽  
M Tyler ◽  
D Boulter
Keyword(s):  
Genetic Variation ◽  
Pisum Sativum ◽  
Storage Protein ◽  
Purification And Characterization ◽  
Native Form ◽  
Pisum Sativum L ◽  
A Subunit ◽  
Cnbr Cleavage ◽  
Pea Seeds

A third storage protein, distinct from legumin and vicilin, has been purified from the seeds of pea (Pisum sativum L.). This protein has been named ‘convicilin’ and is present in protein bodies isolated from pea seeds. Convicilin has a subunit mol.wt. of 71 000 and a mol.wt. in its native form of 290 000. Convicilin is antigenically dissimilar to legumin, but gives a reaction of identity with vicilin when tested against antibodies raised against both proteins. However, convicilin contains no vicilin subunits and may be clearly separated from vicilin by non-dissociating techniques. Unlike vicilin, convicilin does not interact with concanavalin A, and contains insignificant amounts of carbohydrates. Limited heterogeneity, as shown by isoelectric focusing, N-terminal analysis, and CNBr cleavage, is present in convicilin isolated from a single pea variety; genetic variation of the protein between pea lines has also been observed.

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