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PubMed2001

Genes determining pathogenicity to pea are clustered on a supernumerary chromosome in the fungal plant pathogen Nectria haematococca.

Three genes that contribute to the ability of the fungus Nectria haematococca to cause disease on pea plants have been identified. These pea pathogenicity (PEP) genes are within 25 kb of each other and are located on a supernumerary chromosome. Altogether, the PEP gene cluster contains six transcriptional units that are expressed during infection of pea tissue. The biochemical function of only one of the genes is known with certainty. This gene, PDA1, encodes a specific cytochrome P450 that confers resistance to pisatin, an antibiotic produced by pea plants. The three new PEP genes, in addition to PDA1, can independently increase the ability of the fungus to cause lesions on pea when added to an isolate lacking the supernumerary chromosome. Based on predicted amino acid sequences, functions for two of these three genes are hypothesized. The deduced amino acid sequence of another transcribed portion of the PEP cluster, as well as four other open reading frames in the cluster, have a high degree of similarity to known fungal transposases. Several of the features of the PEP cluster -- a cluster of pathogenicity genes, the presence of transposable elements, and differences in codon usage and GC content from other portions of the genome -- are shared by pathogenicity islands in pathogenic bacteria of plants and animals.

Amino Acid Sequence↗

PubMed2005

Differential impact of environmental stresses on the pea mitochondrial proteome.

Exposure to adverse environmental conditions causes oxidative stress in many organisms, leading either to disease and debilitation or to response and tolerance. Mitochondria are a key site of oxidative stress and of cellular response and play important roles in cell survival. We analyzed the response of mitochondria in pea (Pisum sativum) plants to the common stresses associated with drought, cold, and herbicides. These treatments all altered photosynthetic and respiratory rates of pea leaves to various extents, but only herbicides significantly increased lipid peroxidation product accumulation. Mitochondria isolated from the stressed pea plants maintained their electron transport chain activity, but changes were evident in the abundance of uncoupling proteins, non-phosphorylating respiratory pathways, and oxidative modification of lipoic acid moieties on mitochondrial proteins. These data suggest that herbicide treatment placed a severe oxidative stress on mitochondria, whereas chilling and particularly drought were milder stresses. Detailed analysis of the soluble proteome of mitochondria by gel electrophoresis and mass spectrometry revealed differential degradation of key matrix enzymes during treatments with chilling being significantly more damaging than drought. Differential induction of heat shock proteins and specific losses of other proteins illustrated the diversity of response to these stresses at the protein level. Cross-species matching was required for mass spectrometry identification of nine proteins because only a limited number of pea cDNAs have been sequenced, and the full pea genome is not available. Blue-native separation of intact respiratory chain complexes revealed little if any change in response to environmental stresses. Together these data suggest that although many of the molecular events identified by chemical stresses of mitochondria from a range of model eukaryotes are also apparent during environmental stress of plants, their extent and significance can vary substantially.

Cold Temperature↗

PubMed1990

Large bowel fermentation in rats given diets containing raw peas (Pisum sativum).

The digestion of non-starch polysaccharides (NSP) was studied in rats given semi-purified diets containing 0-500 g raw peas (Pisum sativum)/kg. NSP were equally well digested at all inclusion levels with digestibilities for individual constituents ranging from 0.58 for xylans to 0.99 for arabinose-containing polymers with a total NSP digestibility of 0.79. Increasing the dietary pea inclusion rate increased the amount of substrate flowing to the large bowel (LB) and this was associated with marked increases in caecal tissue and contents masses, a reduction in caecal transit time from 0.88 to 0.43 d and a threefold increase in faecal bacterial output. Caecal pH fell as did the molar proportions of acetate, isobutyrate, isovalerate and valerate whilst butyrate increased when peas were included in the diet. Possible mechanisms for these fermentation end-product changes are discussed. Pea inclusion in the diet was associated with increased volatile fatty acid and 3-hydroxy butyrate concentrations in portal and heart blood. It was concluded that peas are a rich source of fermentable polysaccharides which produce a LB fermentation pattern of potential health benefit.

3-Hydroxybutyric Acid↗

PubMed2006

Appetite during consumption of enteral formula as a sole source of nutrition: the effect of supplementing pea-fibre and fructo-oligosaccharides.

Liquid enteral formulas are commonly used as a sole source of nutritional support of patients in hospital and community settings. Their effect on appetite has important consequences for dietary management of such patients and is likely to be affected by the formula composition. The aim of the present study was to compare appetite within healthy subjects consuming both a standard formula and one supplemented with pea-fibre (10 g/l) and fructo-oligosaccharide (FOS; 5 g/l) as a sole source of nutrition. Eleven healthy subjects consumed a standard formula or a pea-fibre/FOS formula as a sole source of nutrition for 14 d in a double-blind, cross-over trial. Appetite was recorded using standard 100 mm lines anchored at each end by a phrase denoting the most extreme appetite sensation. Consumption of the pea-fibre/FOS formula resulted in higher mean fullness (46 v. 37 mm, P=0.035), minimum fullness (13 v. 9 mm, P=0.024) and minimum satiety (12 v. 8 mm, P=0.012) compared to the standard formula. As there were no differences in macronutrient intake between formulas, these differences are likely to be due to supplementation with pea-fibre and FOS. The effect on appetite of the composition of an enteral formula, both with respect to nutrient content and functional components such as pea-fibre and FOS, may be an important aspect to consider in the dietary management of patients consuming enteral formula as a sole source of nutrition.

Adult↗

PubMed1989

Influence of peas (Pisum sativum) as a dietary ingredient and flavomycin supplementation on the performance and intestinal microflora of broiler chicks.

1. Two experiments were carried out to study the effects of diets containing various concentrations of pea meal (Pisum sativum L.), with or without flavomycin supplementation, on the performance and intestinal microflora of broiler chicks. 2. During the 7 to 28-d period, chicks fed on diets containing 300, 600 and 800 g pea meal/kg consumed more food and gained more weight than chicks receiving a maize-isolated soyabean protein control diet. The addition of flavomycin to the diets had similar effects on the performance of both the control and the pea groups. 3. Pea diets, with and without supplemental flavomycin, had little influence on the composition of intestinal microflora. The counts of enterococci in the small intestine and Clostridium perfringens and coliforms in the caeca of pea-fed chicks exceeded those of control chicks.

Aminoglycosides↗

PubMed1988

Inverse correlation between growth and degrading enzyme activity of seedlings after gamma and neutron irradiation of pea seeds.

The effect of gamma-, 14 MeV neutron- and fission neutron irradiation was investigated on the growth rate and degrading enzyme activities of pea seedlings. Both dormant pea seeds and 4-day-old growing seedlings were used for the experiments. Depending on the gamma dose between 15 and 300 Gy the height of pea seedlings was found shorter, and parallel with this the endogenous RNase and peroxidase activities were higher than in the unirradiated controls. Seedlings proved to be more sensitive by about one order of magnitude than seeds. Irradiation of seeds between 5 and 10 Gy slightly enhanced the growth rate of seedlings (10 per cent) and parallel with this, the RNase activity measured was lower than that in the controls. On irradiation of seedlings with 14 MeV neutrons the growth inhibition and RNase activity enhancement was only 1.3 times more effective than in the case of irradiation of seeds. The following RBE values were obtained after irradiation of seeds, related to the biological effect of gamma rays: in growth inhibition, 6 for 14 MeV neutrons and 12 for fission neutrons, and the enhancement of two enzyme activities was 15-30 for 14 MeV neutrons and 45-58 for fission neutrons. In the case of seedling irradiation with 14 MeV neutrons the RBE was 1.0 for growth inhibition and between 3 and 6 for enhancement of enzyme activity. The isoenzyme pattern of RNase also changed: two isoenzymes became predominant after the gamma irradiation of seeds, characterized by molecular weights of 21,000 and 30,000, respectively. As a result of enhanced RNase activity, the degradation of longer polysomes to monomeric ribosomes occurred. Thus after ionizing irradiation of pea seeds and seedlings an inverse correlation was found between the growth rate of pea seedlings and the activities of degrading enzymes.

Cobalt Radioisotopes↗

PubMed1999

Purification of catalase from pea leaf peroxisomes: identification of five different isoforms.

Catalase activity was analyzed in seven organs of pea (Pisum sativum L.) plants: leaves, seeds, flowers, shoots, whole fruits, pods and roots. Leaves showed the highest activity followed by whole fruits and flowers. Catalase was purified from pea leaf peroxisomes. These organelles were isolated from leaves by differential and sucrose density-gradient centrifugation, and catalase was purified by two steps involving anion exchange and hydrophobic chromatography using a Fast Protein Liquid Chromatography system. Pure catalase had a specific activity of 953 mmol H2O2 min(-1) mg(-1) protein and was purified 1000-fold, with a yield of about 19 microg enzyme per kg of pea leaves. Analysis by SDS-PAGE and immunoblot showed that the pea catalase was composed of subunits of 57 kDa. Ultraviolet and visible absorption spectra of the enzyme showed two absorption maxima at 252 and 400 nm with molar extinction coefficients of 2.14 x 10(6) and 7.56 x 10(6) M(-1) cm(-1), respectively. By isoelectric focusing (pH 5-7), five different isoforms were identified and designated as CAT1-5, with isoelectric points of 6.41, 6.36, 6.16, 6.13 and 6.09, respectively. All the catalase isoforms contained a subunit of 57 kDa. Post-embedment, EM immunogold labelling of catalase showed a uniform distribution of the enzyme inside the matrix and core of pea leaf peroxisomes.

Catalase↗

PubMed2003

Comparison of the effects of dried peas with those of potatoes in mixed meals on postprandial glucose and insulin concentrations in patients with type 2 diabetes.

BACKGROUND: Data on the blood glucose response of diabetic patients to mixed meals containing food both rich in fiber and with a low glycemic index, such as dried peas, is scarce. Thus, the extent to which type 2 diabetic patients should take into account low-glycemic, high-fiber foods for their daily carbohydrate intake is uncertain. OBJECTIVE: We compared the glycemic and insulinemic responses to 3 different meals based on dried peas, potatoes, or both in patients with type 2 diabetes undergoing dietary treatment. DESIGN: The meals, prepared according to local recipes and consumed at weekly intervals in random order at lunchtime, contained comparable amounts of carbohydrate, fat, protein, and water. The carbohydrate source of the meals differed and was supplied from either dried peas (meal 1), potatoes (meal 3), or a combination thereof (meal 2). Peripheral and venous blood was sampled over 180 min. RESULTS: The increases in postprandial plasma glucose and insulin concentrations were delayed and significantly smaller after the pea meal than after the potato meal. The areas under the glucose curve were 164 +/- 40, 257 +/- 57, and 381 +/- 40 mmol x 180 min/L for meals 1, 2, and 3, respectively (P < 0.01). The areas under the insulin curve were 13.8 +/- 4.3, 15.4 +/- 3.9, and 31.2 +/- 6.9 nmol x 180 min/L, respectively (P = 0.0514). CONCLUSION: These findings suggest that carbohydrates in dried peas may be largely disregarded in carbohydrate counting and that type 2 diabetic patients should probably increase their consumption of low-glycemic, high-fiber foods at the expense of high-glycemic, low-fiber foods.

Aged↗

PubMed2002

Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain.

PEA-15 is a multifunctional protein that modulates signaling pathways which control cell proliferation and cell death. In particular, PEA-15 regulates the actions of the ERK MAP kinase cascade by binding to ERK and altering its subcellular localization. The three-dimensional structure of PEA-15 has been determined using NMR spectroscopy and its interaction with ERK defined by characterization of mutants that modulate ERK function. PEA-15 is composed of an N-terminal death effector domain (DED) and a C-terminal tail of irregular structure. NMR 'footprinting' and mutagenesis identified elements of both the DED and tail that are required for ERK binding. Comparison of the DED-binding surface for ERK2 with the death domain (DD)-binding surface of Drosophila Tube revealed an unexpected similarity between the interaction modes of the DD and DED motifs in these proteins. Despite a lack of functional or sequence similarity between PEA-15 and Tube, these proteins utilize a common surface of the structurally similar DD and DED to recognize functionally diverse targets.

Amino Acid Motifs↗

PubMed2003

Granary trial of protein-enriched pea flour for the control of three stored-product insects in barley.

A granary trial was conducted to evaluate the efficacy of protein-enriched pea flour against three common stored-grain insects, Sitophilus oryzae (L.), Tribolium castaneum (Herbst), and Cryptolestes ferrugineus (Stephens). Six 30-t farm granaries were filled with approximately 11 t of barley. The barley was either not treated, treated with protein-enriched pea flour at 0.1% throughout the entire grain mass, or treated at 0.5% throughout the top half of the grain mass. Adult insects were released in screened boxes (two insects per kilogram barley for S. oryzae and T. castaneum 1.4 insects per kilogram barley for C. ferrugineus). Barley was sampled four times during the 70-d trial. The number and mortality of adults and emerged adults in the samples were noted. Four kinds of traps, flight, surface-pitfall, probe-pitfall, and sticky-bar, were placed at different locations in the granaries to estimate the movement of insects. The 0.1% protein-enriched pea flour treatment reduced adult numbers of S. oryzae by 93%, T. castaneum by 66%, and C. ferrugineus by 58%, and reduced the emerged adults by 87, 77, and 77%, respectively. Treating the top half of the barley with 0.5% protein-enriched pea flour had similar effects as treating the entire grain mass with 0.1% pea-protein flour. However, the top-half treatment failed to prevent insects from penetrating into the untreated lower layer. Differences between traps are discussed.

Animals↗

PubMed2001

Differential antioxidative responses to cadmium in roots and leaves of pea (Pisum sativum L. cv. Azad).

Pea (Pisum sativum L. cv. Azad) plants exposed to 4 and 40 microM of Cd for 7 d in hydroponic culture were analysed with reference to the distribution of metal, the accumulation of biomass and the metal's effects on antioxidants and antioxidative enzymes in roots and leaves. Cd-induced a decrease in plant biomass. The maximum accumulation of Cd occurred in roots followed by stems and leaves. An enhanced level of lipid peroxidation and an increased tissue concentration of hydrogen peroxide (H2O2) in both roots and leaves indicated that Cd caused oxidative stress in pea plants. Roots and leaves of pea plants responded differently to Cd with reference to the induction of enhanced activities of most of the enzymes monitored in the present study. These differential responses to Cd were further found to be associated with levels of Cd to which the plants were exposed. Cd-induced enhancement in superoxide dismutase (SOD) activity was more at 40 microM than at 4 microM in leaves. While catalase (CAT) prominently increased in leaves both at 4 and 40 microM Cd, ascorbate peroxidase (APX) showed maximum stimulation at 40 microM Cd in roots. Enhancement in glutathione reductase (GR) activity was also more at 40 microM than at 4 microM Cd in roots. While glutathione peroxidase (GPOX) activity decreased in roots and remained almost unmodified in leaves, glutathione S-transferase (GST) showed pronounced stimulation in both roots and leaves of pea plants exposed to 40 microM Cd. Increased activities of antioxidative enzymes in Cd-treated plants suggest that they have some additive function in the mechanism of metal tolerance in pea plants.

Antioxidants↗

PubMed1983

U1, U2 and U5 small nuclear RNAs are found in plants cells. Complete nucleotide sequence of the U5 RNA family from pea nuclei.

U1, U2 and U5 RNAs were isolated from pea nuclei with antibody specific for 2,2,7-trimethylguanosine. The nucleotide sequence of the 3'-terminal halves of pea U1 and U2 snRNAs and the complete sequence of five out of the six U5 RNA variants isolated is given. The high number of U5 variants suggest they are encoded by a multigene family containing at least six different genes. Similar secondary structures could be derived for all of the pea U5 RNAs and although the degree of sequence conservation between plant and vertebrate U5 RNAs is as low as 35%, nearly identical secondary structures can be proposed for both RNA groups. All the snRNA species U1, U2 and U5 from pea share a structural domain, the so-called domain A, which is also common to all animal snRNA U1, U2, U4 and U5. Furthermore, a block of 22 consecutive nucleotides is conserved among pea and vertebrate U5 RNAs, from which 11 nucleotides constitute a hairpin-loop with a high number of posttranscriptional modifications. We propose that conservation of this hairpin-loop, together with domain A, is of prime importance for the functioning of U5 RNAs in plant and animal cells.

Base Sequence↗

PubMed1985

Pea cytochrome oxidase subunit II gene has no intron and generates two mRNA transcripts with different 5'-termini.

We have isolated and sequenced the cytochrome oxidase subunit II (COII) gene from pea mitochondria. The coding sequence (777 bp) shows over 90% homology to the COII genes from three monocotyledonous plants (rice, maize and wheat) and one dicotyledonous plant (Oenothera berteriana). Several codons are deleted, however, in the pea COII gene. Of interest is the deletion in pea of the last three codons, including the stop codon, found at the 3' end of the other four COII genes. Instead, a new stop codon has been created due to a single-base substitution at the 13th bp downstream from the position of the original stop codon. This pea gene does not contain an intron which is found in all three monocots. Two distinct 5' termini of the pea COII transcripts have been identified by S1 nuclease mapping, one at 285 bp (site I) and the other at 302 bp (site II) upstream from the ATG codon. They are located at two identical sites within nearly perfect direct repeats. Transcripts with the 5' end corresponding to site I occur five time more frequently than those with the 5' end corresponding to site II. Both transcripts have the same 3' terminus which has been mapped to be at 193 to 195 bp downstream from the stop codon.

Base Sequence↗

PubMed1999

Functional analysis of retrotransposons in pea.

The 5'-upstream regions of the plant active defense genes in pea (PSPAL2 and PSCHS1) exhibit significant nucleotide sequence identity to part of a copia-type retrotransposon. To characterize the retrotransposon in pea putative reverse transcriptase sequences (Psr) were amplified by PCR from cDNA prepared from protoplasts derived from pea suspension cultured cells. Psr genes can be classified into at least eight subgroups (A-H) according to their nucleotide sequence similarities. A subgroup PsrC was induced by the treatment of etiolated pea epicotyls with fungal elicitor within 30 min but was hardly induced by protoplasting of pea suspension cultured cells, whereas subgroups of PsrA and PsrB were highly induced by protoplasting. Interestingly, the retrotransposon sequence present at the 5'-upstream region of PSCHS1 which was induced by the treatment with fungal elicitor belonged to subgroup PsrC. The retrotransposon might play an important role in reorganization of the genes and optimization of the gene expression in response to various environmental stimuli such as an attack by phytopathogens or protoplasting.

5' Untranslated Regions↗

PubMed2001

The molecular characterization and in situ expression pattern of pea SCARECROW gene.

Certain mutants of shoot gravitropism were reported to be ascribed to the SCR and SHR loci in Arabidopsis thaliana. The SCR gene was known to regulate the development of endodermis cells that are responsible for sensing gravity in a shoot. With the aim of elucidating the molecular mechanism for gravitropic responses in pea seedlings, we have isolated a putative pea SCR ortholog from a shoot cDNA library. Analyses of the cDNA clones revealed the structure of a full-length ORF coding for 819 amino acid residues. A remarkable feature of pea SCR protein was the presence of asparagine stretches at the N-terminal transcriptional activation domain, which was distinct from the occurrence of glutamine or alanine stretches in the Arabidopsis or maize SCR. A Northern blot analysis revealed a single 3.2-kb pea SCR transcript in addition to a closely related 2.5-kb transcript. Our in situ hybridization data indicated that pea SCR mRNA accumulated in the shoot apical meristem, leaf primordia and a root single cell layer corresponding to the endodermis. The expression patterns were similar to those reported for A. thaliana and Zea mays, suggesting that SCR may be functionally conserved among plants and involved in the differentiation of the endodermis.

Amino Acid Sequence↗

PubMed2005

Nutritive values of corn, soybean meal, canola meal, and peas for broiler chickens as affected by a multicarbohydrase preparation of cell wall degrading enzymes.

The effect of a new multicarbohydrase supplement of cell wall degrading activities on the nutritive value of corn, soybean meal (SBM), canola meal (CM), and peas for broiler chickens was investigated. Four isoenergetic and isonitrogenous corn (69% corn), SBM (30% SBM, 59% corn), CM (30% CM, 54% corn), and pea (30% peas, 52% corn) diets, without or with enzyme supplementation, were formulated to meet NRC specifications for broiler chickens (except for AME and CP, which were at 95 and 92% of NRC requirements, respectively). The enzyme supplement supplied 1,000 U of xylanase, 400 U of glucanase, 1,000 U of pectinase, 120 U of cellulase, 280 U of mannanase, and 180 U of galactanase per kilogram of diet. Each diet was fed in a mash form to 9 replicate pens of 5 broilers from 5 to 18 d. When compared with the control treatment, enzyme addition to the corn diet improved (P < 0.05) feed-to-gain ratio, whereas the performance of birds fed the other 3 diets was not affected. An increase (P < 0.05) in total tract nonstarch polysaccharides (NSP) digestibility, ileal starch digestibility, and AMEn was observed in birds fed the enzyme-supplemented corn diet. An improvement (P < 0.05) in total tract NSP digestibility, ileal protein digestibility, and AMEn content with enzyme supplementation was observed for the SBM diet. However, nutrient digestibilities and AMEn of CM and pea diets were not affected (P > 0.05) by enzyme addition even though the NSP digestibilities increased significantly (P < 0.05). A significant increase (P < 0.05) in water-soluble NSP and a decrease (P < 0.05) in water-insoluble NSP concentration of ileal digesta was noted for birds fed all 4 enzyme-supplemented diets. It would appear from this study that the nutrient utilization of corn-SBM diet by broilers could be enhanced by using an appropriate multicarbohydrase enzyme supplement. The nutrient encapsulating effect of cell wall polysaccharides in SBM, CM, and peas may not be the only factor responsible for incomplete nutrient utilization. The improvement in feed efficiency and starch availability in birds fed corn diet likely resulted from the cell wall degrading activity of the enzyme supplement.

Animal Feed↗

PubMed1998

Potyvirus genome-linked protein (VPg) determines pea seed-borne mosaic virus pathotype-specific virulence in Pisum sativum.

The mechanism of Pisum sativum pathotype-specific resistance to pea seed-borne mosaic potyvirus (PSbMV) was investigated and the coding region determinant of PSbMV virulence was defined. Homozygous recessive sbm-1 peas are unable to support replication of PSbMV pathotype 1 (P-1), whereas biochemically and serologically related pathotype 4 (P-4) is fully infectious in the sbm-1/sbm-1 genotype. We were unable to detect viral coat protein or RNA with double antibody sandwich-enzyme-linked immunosorbent assay and reverse transcription-polymerase chain reaction in sbm-1/sbm-1 P-1-inoculated protoplasts and plants. Lack of viral coat protein or RNA in P-1 transfected sbm-1/sbm-1 protoplasts suggests that sbm-1 resistance is occurring at the cellular level and that inhibition of cell-to-cell virus movement is not the operating form of resistance. In addition, because virus products were not detected at any time post-inoculation, resistance must either be constitutive or expressed very early in the virus infection process. P-1-resistant peas challenged with full-length, infectious P-1/P-4 recombinant clones demonstrated that a specific P-4 coding region, the 21-kDa, genome-linked protein (VPg), was capable of overcoming sbm-1 resistance, whereas clones containing the P-1 VPg coding region were noninfectious to sbm-1/sbm-1 peas. VPg is believed to be involved in potyvirus replication and its identification as the PSbMV determinant of infectivity in sbm-1/sbm-1 peas is consistent with disruption of an early P-1 replication event.

Amino Acid Sequence↗

PubMed2001

Root mucilage from pea and its utilization by rhizosphere bacteria as a sole carbon source.

Plant roots secrete a complex polysaccharide mucilage that may provide a significant source of carbon for microbes that colonize the rhizosphere. High molecular weight mucilage was separated by high-pressure liquid chromatography gel filtration from low molecular weight components of pea root exudate. Purified pea root mucilage generally was similar in sugar and glycosidic linkage composition to mucilage from cowpea, wheat, rice, and maize, but appeared to contain an unusually high amount of material that was similar to arabinogalactan protein. Purified pea mucilage was used as the sole carbon source for growth of several pea rhizosphere bacteria, including Rhizobium leguminosarum 8401 and 4292, Burkholderia cepacia AMMD, and Pseudomonas fluorescens PRA25. These species grew on mucilage to cell densities of three- to 25-fold higher than controls with no added carbon source, with cell densities of 1 to 15% of those obtained on an equal weight of glucose. Micromolar concentrations of nod gene-inducing flavonoids specifically stimulated mucilage-dependent growth of R. leguminosarum 8401 to levels almost equaling the glucose controls. R. leguminosarum 8401 was able to hydrolyze p-nitrophenyl glycosides of various sugars and partially utilize a number of purified plant polysaccharides as sole carbon sources, indicating that R. leguminosarum 8401 can make an unexpected variety of carbohydrases, in accordance with its ability to extensively utilize pea root mucilage.

Amino Acids↗