Effects of medium osmolarity on the release of amino acids from isolated cotyledons of developing pea seeds

Planta ◽  
1990 ◽  
Vol 181 (4) ◽  
Author(s):  
FrankC. Lanfermeijer ◽  
JudithW. Koerselman-Kooij ◽  
AdrianusC. Borstlap
Keyword(s):  
Amino Acids ◽  
Medium Osmolarity ◽  
Pea Seeds

Fungal antisporulant activity of a complex lipid fraction extracted from pea seeds

1975 ◽  
Vol 53 (16) ◽  
pp. 1625-1629 ◽  
Author(s):  
F. L. Pfleger ◽  
G. E. Harman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Alternaria Alternata ◽  
Lipid Fraction ◽  
Aphanomyces Euteiches ◽  
Complex Lipid ◽  
Ascochyta Pisi ◽  
Pea Seeds ◽  
The Mean ◽  
Race 2

A substance was isolated from dry whole pea seeds (Pisum sativum 'Alaska') that inhibited sporulation, but not growth, of Alternaria alternata, Aspergillus ruber, Ascochyta pisi, Phyllosticta antirrhini, Rhizoctonia solani, Nectria haematococca var. cucurbitae, and Fusarium oxysporum f. sp. pisi race 2. The substance had no effect on sporulation or growth of Aphanomyces euteiches. The mean effective dose (ED50) of the partially purified material was 30 μg/ml when tested against Alternaria alternata. The partially purified substance was soluble in petroleum ether, chloroform, and hexane but formed an emulsion in water. The partially purified material contained amino acids, lipids, phosphorus, and carbohydrate. Its molecular weight was in excess of 14 000. These properties indicate that it is a complex lipid with properties similar to many proteolipids.

scholarly journals Biosynthesis of willardiine and isowillardiine in germinating pea seeds and seedlings

1972 ◽  
Vol 129 (4) ◽  
pp. 897-905 ◽  
Author(s):  
T. S. Ashworth ◽  
E. G. Brown ◽  
F. M. Roberts
Keyword(s):  
Amino Acids ◽  
Side Chain ◽  
Free Base ◽  
Pyrimidine Metabolism ◽  
Uracil Derivatives ◽  
Weak Activity ◽  
Pea Seeds

The synthesis of the pyrimidinyl amino acids willardiine and isowillardiine was studied in vivo and in vitro. Uracil derivatives stimulate the biosynthesis of both compounds; the free base is the most effective. Significant incorporation of [2-14C]uracil and [6-14C]orotate into willardiine and isowillardiine was found. Incorporation of [6-14C]orotate was substantially decreased in the presence of uracil, and to a lesser extent by uridine and UMP. [3-14C]Serine was incorporated into the alanine side chain of the two uracilylalanines but not into the ring. The effect of a number of uracil analogues and inhibitors of pyrimidine metabolism was examined. Some were shown to stimulate the biosynthesis; the most noticeable effects were obtained with 6-azauracil and 2-thiouracil. Attempts to obtain extracts capable of synthesizing the uracilylalanines from uracil and serine were unsuccessful, but weak activity was observed when serine was replaced by O-acetylserine.

scholarly journals Role of pfkA and General Carbohydrate Catabolism in Seed Colonization by Enterobacter cloacae

1999 ◽  
Vol 65 (6) ◽  
pp. 2513-2519 ◽  
Author(s):  
D. P. Roberts ◽  
P. D. Dery ◽  
I. Yucel ◽  
J. Buyer ◽  
M. A. Holtman ◽  
...  
Keyword(s):  
Amino Acids ◽  
Sweet Corn ◽  
Carbon Sources ◽  
Enterobacter Cloacae ◽  
In Vitro Growth ◽  
Wild Type ◽  
Exogenous Addition ◽  
Total Carbohydrates ◽  
Pea Seeds

ABSTRACT Enterobacter cloacae A-11 is a transposon mutant of strain 501R3 that was deficient in cucumber spermosphere colonization and in the utilization of certain carbohydrates (D. P. Roberts, C. J. Sheets, and J. S. Hartung, Can. J. Microbiol. 38:1128–1134, 1992). In vitro growth of strain A-11 was reduced or deficient on most carbohydrates that supported growth of strain 501R3 but was unaffected on fructose, glycerol, and all amino acids and organic acids tested. Colonization by strain A-11 was significantly reduced (P ≤ 0.05) for cucumber and radish seeds compared to that of strain 501R3, but colonization of pea, soybean, sunflower, and sweet corn seeds was not reduced. Pea seeds released several orders of magnitude more total carbohydrates and amino acids than cucumber and radish seeds and approximately 4,000-fold more fructose. Fructose was the only carbohydrate detected in the seed exudates which supported wild-type levels of in vitro growth of strain A-11. Soybean, sunflower, and sweet corn seeds also released significantly greater amounts of fructose and total carbohydrates and amino acids than cucumber or radish seeds. The exogenous addition of fructose to cucumber and radish seeds at quantities similar to the total quantity of carbohydrates released from pea seeds over 96 h increased the populations of strain A-11 to levels comparable to those of strain 501R3 in sterile sand. Molecular characterization of strain A-11 indicated that the mini-Tn5 kanamycin transposon was inserted in a region of the genome with significant homology topfkA, which encodes phosphofructo kinase. A comparison of strain A-11 with Escherichia coli DF456, a knownpfkA mutant, indicated that the nutritional loss phenotypes were identical. Furthermore, the pfkA homolog cloned fromE. cloacae 501R3 complemented the nutritional loss phenotypes of both E. coli DF456 and E. cloacaeA-11 and restored colonization by strain A-11 to near wild-type levels. These genetic and biochemical restoration experiments provide strong evidence that the quantities of reduced carbon sources found in seed exudates and the ability of microbes to use these compounds play important roles in the colonization of the spermosphere.

scholarly journals Standardised Ileal Amino Acid Digestibility in Field Pea Seeds of Two Cultivars Differing in Flower Colour for Broiler Chickens: Effects of Bird Age and Microbial Protease

Animals ◽  
2020 ◽  
Vol 10 (11) ◽  
pp. 2099
Author(s):  
Witold Szczurek ◽  
Sylwester Świątkiewicz
Keyword(s):  
Amino Acids ◽  
Broiler Chickens ◽  
Flower Colour ◽  
Field Pea ◽  
Apparent Digestibility ◽  
Ileal Digestibility ◽  
Microbial Protease ◽  
Significant Difference ◽  
Pea Seeds

This study aimed to determine and compare standardised ileal digestibility (SID) coefficients of amino acids (AA) in raw seeds of the white-(WF) and the coloured-flowered (CF) field pea cultivar as sole sources of AA in the diets fed to broiler chickens aged 14 or 28 days. An additional purpose was to check the influence of exogenous protease added to pea-based assay diets on AA SID in birds at both ages. Each assay diet was offered to six replicate pens. On both sampling days, the contents from the lower half of the ileum were collected for determination of the apparent digestibility values. The SID coefficients were calculated using ileal endogenous AA losses determined from birds fed an N-free diet. Results indicated a substantial advantage of WF pea over CF pea as a source of digestible Lys, Met, Cys, His, Ile, Leu, Phe, Val, Asp and Glu for 14-day-old chickens. With the exception of methionine and cysteine, there was no significant difference between these two cultivars in the SID values of AA in 28-day-old birds. The protease increased SID of nutritionally essential AA from WF pea-based diet at both ages, and from CF pea-based diet in chickens aged 28 days. In conclusion, the SID coefficients of indispensable AA determined at 14 days of age in low-tannin WF peas are not applicable to the formulation of grower-type feeds containing seeds of CF cultivars.

Amino acid sequence differences in the alpha chains of pea seed isolectins: C-terminal processing

1987 ◽  
Vol 65 (4) ◽  
pp. 338-344 ◽  
Author(s):  
James Michael Rini ◽  
Theo Hofmann ◽  
Jeremy P. Carver
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Cdna Clone ◽  
Edman Degradation ◽  
Pea Seeds ◽  
Pea Seed

The complete amino acid sequence of the alpha chains of both isolectins found in pea seeds has been determined using automated Edman degradation. We show that the alpha chains of these two proteins differ only at their C-termini: isolectin B is two amino acids longer than isolectin A. Furthermore, the alpha chains of both isolectins are shorter than would be predicted from the nucleotide sequence of a cDNA clone for pea lectin. We suggest, therefore, that these proteins arise from differential C-terminal processing. Amino acid composition data and C-terminal analysis show that the beta chains have also been processed at their C-termini, but in this case identical chains for both isolectins are produced.

scholarly journals Aminopeptidases of pea

1974 ◽  
Vol 141 (1) ◽  
pp. 113-118 ◽  
Author(s):  
T. C. Elleman
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Free Amino ◽  
The Other ◽  
Amide Bond ◽  
Amino Group ◽  
Amide Bonds ◽  
Primary Amino ◽  
Pea Seeds ◽  
Hydrolysis Of

Studies of crude extracts of pea seeds (Pisum sativum, var. Green feast) revealed the presence of three enzymes that hydrolyse the amide bond of aminoacyl β-naphthylamides. They differ in their specificity towards the aminoacyl moiety; one is proline-specific, whereas the other two hydrolyse the β-naphthylamides of primary amino acids. Of the latter, one is highly specific for hydrophobic aminoacyl residues whereas the other has a broader, somewhat complementary specificity, showing preferential hydrolysis of non-hydrophobic aminoacyl residues. These latter two aminoacyl-β-naphthylamidases have been separated and partly characterized with regard to substrate specificity and antagonism by inhibitors. Both are true aminopeptidases, requiring the presence of a free amino group and hydrolysing the amide bonds of amino acid amides, dipeptides and oligopeptides consecutively from the N-terminal end.

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