Determination of pea (Pisum sativum L.) root lectin using an enzyme-linked immunoassay

Planta ◽  
1984 ◽  
Vol 161 (4) ◽  
pp. 302-307 ◽  
Author(s):  
C. L. Díaz ◽  
P. Lems-van Kan ◽  
I. A. M. Van der Schaal ◽  
J. W. Kijne
Keyword(s):  
Pisum Sativum ◽  
Pisum Sativum L ◽  
Root Lectin

Pea (Pisum sativum L.) seed isolectins 1 and 2 and pea root lectin result from carboxypeptidase-like processing of a single gene product

1994 ◽  
Vol 24 (1) ◽  
pp. 75-81 ◽  
Author(s):  
Flip J. Hoedemaeker ◽  
Michael Richardson ◽  
Clara L. Díaz ◽  
B. Sylvia de Pater ◽  
Jan W. Kijne
Keyword(s):  
Pisum Sativum ◽  
Gene Product ◽  
Single Gene ◽  
Pisum Sativum L ◽  
Pea Root ◽  
Root Lectin

Determination of Stelar Elements in Roots of Pisum sativum L.

1982 ◽  
Vol 50 (6) ◽  
pp. 757-762 ◽  
Author(s):  
M. A. RANA ◽  
P. B. GAHAN
Keyword(s):  
Pisum Sativum ◽  
Pisum Sativum L

Oxygen limitation of N2 fixation in various legume symbioses

1994 ◽  
Vol 74 (4) ◽  
pp. 853-855 ◽  
Author(s):  
B. N. Kaiser ◽  
B. J. Shelp ◽  
P. Thumfort ◽  
D. B. Layzell
Keyword(s):  
Nitrogen Fixation ◽  
Glycine Max ◽  
Phaseolus Vulgaris ◽  
Pisum Sativum ◽  
Oxygen Limitation ◽  
Phaseolus Vulgaris L ◽  
Pisum Sativum L ◽  
Glycine Max L ◽  
Legume Nitrogen Fixation

Two O2 ramping techniques (linear versus exponential) were used to investigate the response of H2 evolution from intact nodules of soybean (Glycine max (L.) Merr. 'Maple Arrow'), stem-girdled soybean, pea (Pisum sativum L. 'Juneau'), and common bean (Phaseolus vulgaris L. 'Ex Rico 23') to increasing O2 concentrations from 20 to 100% over a 30-min period. The data indicate symbiosis-specific responses to the two ramps, and possible implications for determination of O2 limitation of N2 fixation. Key words: Hydrogen evolution, legume, nitrogen fixation

Determination of Lectins in Root Slime and Root Cell Wall Preparations of Pisum sativum L.

1984 ◽  
pp. 414-414
Author(s):  
Clara L. Díaz ◽  
Ton J. van Driel ◽  
Ineke A. M. van der Schaal ◽  
Jan W. Kijne
Keyword(s):  
Cell Wall ◽  
Pisum Sativum ◽  
Root Cell ◽  
Pisum Sativum L ◽  
Root Cell Wall

Determination of green forage and silage protein degradability of some pea (Pisum sativum L.) + oat (Avena sativa L.) mixtures grown in Serbia

2017 ◽  
Vol 23 (4) ◽  
Author(s):  
Milomir Blagojević ◽  
Nenad Đorđević ◽  
Bora D ◽  
Jordan Marković ◽  
Tanja Vasić ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Avena Sativa ◽  
Pisum Sativum L ◽  
Protein Degradability

scholarly journals Purification and kinetic analysis of pea (Pisum sativum L.) NADPH:protochlorophyllide oxidoreductase expressed as a fusion with maltose-binding protein in Escherichia coli

1997 ◽  
Vol 325 (1) ◽  
pp. 139-145 ◽  
Author(s):  
Giles E. M. MARTIN ◽  
Michael P. TIMKO ◽  
Helen M. WILKS
Keyword(s):  
Escherichia Coli ◽  
Pisum Sativum ◽  
Molecular Mass ◽  
Binding Protein ◽  
Maltose Binding Protein ◽  
Cell Protein ◽  
Kinetic Properties ◽  
Nadph:Protochlorophyllide Oxidoreductase ◽  
Pisum Sativum L

NADPH:protochlorophyllide oxidoreductase (POR) catalyses the light-dependent reduction of protochlorophyllide to chlorophyllide, a key reaction in the chlorophyll biosynthetic pathway. To facilitate structure–function studies, POR from pea (Pisum sativum L.) has been overexpressed in Escherichia coli as a fusion with maltose-binding protein (MBP) at 5–10% of the total soluble cell protein. The fusion protein (MBP–POR) has been purified to greater than 90% homogeneity by a two-step affinity-purification procedure. This represents the first successful overexpression and purification of a plant POR. MBP–POR was found to be active, and the kinetic properties were determined using a continuous assay in which the rate of chlorophyllide formation was measured. The Vmax was 20.6± 0.9 nmol·min-1·mg-1 and the Km values for NADPH and protochlorophyllide were 8.7±1.9 μM and 0.27±0.04 μM respectively. These results represent the first determination of the kinetic properties of a pure POR and the first report on the kinetics of POR from a dicotyledenous plant. The experiments described here demonstrate that the enzyme is not a ‘suicide’ enzyme, and the only components required for catalysis are NADPH, protochlorophyllide and light. Size-exclusion chromatography on a Superose 6 HR column indicated that MBP–POR has a molecular mass of 155 kDa (compared with the molecular mass of 80 kDa estimated by SDS/PAGE), indicating that it behaves as a dimer in solution. This is the first direct determination of the oligomerization state of POR.

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