Purification and properties of CTP:cholinephosphate cytidylyltransferase from pea (Pisum sativum L.)

1985 ◽  
Vol 13 (6) ◽  
pp. 1243-1244 ◽  
Author(s):  
MOLLY J. PRICE-JONES ◽  
JOHN L. HARWOOD
Keyword(s):  
Pisum Sativum ◽  
Pisum Sativum L ◽  
Purification And Properties

scholarly journals Purification and properties of asparaginase from the testa of immature seeds of pea (Pisum sativum L.)

2001 ◽  
Vol 44 (3) ◽  
pp. 239-245 ◽  
Author(s):  
Eliana P. Chagas ◽  
Ladaslav Sodek
Keyword(s):  
Pisum Sativum ◽  
Competitive Inhibition ◽  
Native Page ◽  
Protein Affinity ◽  
Pisum Sativum L ◽  
Crude Extracts ◽  
Purification And Properties ◽  
Sds Page ◽  
Immature Seeds ◽  
Pea Seeds

A K+-dependent asparaginase (E.C. 3.5.1.1.) was purified 1328-fold from the testas of immature pea seeds (Pisum sativum L., var. Bolero) and characterized. Antibodies raised against purified asparaginase cross-reacted with the putative asparaginase band in Western blot analyses of semi-purified extracts. However, for crude extracts of pea testas, a cross-reaction was obtained with at least four protein bands, one of which was asparaginase protein. Affinity-purified antibodies to the four strongest bands of crude extracts were fairly specific for the bands from which they were purified, suggesting a mixture of specific antibodies. The Mr of asparaginase was 69,000 by Sephacryl S200 chromatography and also by mobility on native PAGE relative to BSA. There was no evidence for dissociation into subunits on SDS-PAGE, suggesting a monomeric protein of Mr 69,000. Other properties include an apparent Km of 2.4 mM, pI between 4.5 and 5, and competitive inhibition by aspartate and glycine.

scholarly journals Partial purification and properties of carbamoyl phosphate synthetase of Alaska pea (Pisum sativum L. cultivar Alaska). Purification and general properties

1969 ◽  
Vol 113 (2) ◽  
pp. 271-279 ◽  
Author(s):  
T. Denny O'neal ◽  
Aubrey W. Naylor
Keyword(s):  
Pisum Sativum ◽  
Ammonium Sulphate ◽  
Partial Purification ◽  
Carbamoyl Phosphate Synthetase ◽  
Carbamoyl Phosphate ◽  
Pisum Sativum L ◽  
Low Concentrations ◽  
Purification And Properties ◽  
Phosphate Donor ◽  
Increased Activity

1. Carbamoyl phosphate synthetase was purified up to 45-fold from Alaska pea seedling (Pisum sativum L. cultivar Alaska). 2. The enzyme was most active with and had the lowest Km for l-glutamine as compared with NH4+. 3. The purest preparations utilized very poorly or not at all l-asparagine and urea as nitrogen donors. 4. At saturating concentrations of components of the reaction, the Km for l-glutamine was 1·2×10−4m, and the Km for ATP was approx. 3·9×10−4m. 5. Although the enzyme was very labile, stability was improved by glutamine, asparagine, ammonium sulphate, dithiothreitol and especially l-ornithine. 6. Free ATP was markedly inhibitory, and MgATP2− and Mg2+ appeared to be the actual substrates utilized. 7. Fe2+ and Mn2+ were also utilized, but not as readily as Mg2+ except at low concentrations. K+ increased activity significantly. 8. Of the four nucleotides tested (ITP, ATP, GTP and UTP) only ATP served as an effective phosphate donor.

Mitigation Effects of 24-Epibrassinolide and Thiourea in Field Pea (Pisum sativum L.) under Drought Stress

2018 ◽  
Vol 34 (2) ◽  
pp. 229-235 ◽  
Author(s):  
Prachi Garg ◽  
◽  
A. Hemantaranjan ◽  
Jyostnarani Pradhan ◽  
◽  
...  
Keyword(s):  
Drought Stress ◽  
Pisum Sativum ◽  
Field Pea ◽  
Pisum Sativum L

МЕТОД ЭКСПРЕСС-ОЦЕНКИ АЛЮМОТОЛЕРАНТНОСТИ У ГОРОХА ПОСЕВНОГО (Pisum sativum L.)

2015 ◽  
Vol 50 (3) ◽  
pp. 353-360
Author(s):  
М.А. ВИШНЯКОВА ◽  
◽  
Е.В. СЕМЕНОВА ◽  
И.А. КОСАРЕВА ◽  
Н.Д. КРАВЧУК ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Pisum Sativum L
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