Amino Acids and Derivatives

Brenner, M.; Niederwieser, A.; Pataki, György

doi:10.1007/978-3-642-88488-7_25

Cited by 72 publications

(29 citation statements)

References 172 publications

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“…Leaf samples were collected randomly after 20th day of the spray. Change in total protein contents in leaves was measured by the method of Lowry et al (1951), carbohydrate (Yemm and Willis, 1954), Amino acid (Brenner et al, 1969) and total phenols (Swain and Hillis, 1959). Earma photic 100 spectrophotometer was used for each analysis and quantity was expressed in mg/gm fresh weight using standard curves.…”

Section: Methodsmentioning

confidence: 99%

Effects of Systemic Fungicides on Nutritive Composition of Diseased and Healthy Plants of Triticum aestivum L.

Siddiqui¹,

Ahmed²

2000

Pakistan J. of Biological Sciences

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Application of systemic fungicides showed significant (p<0.001) decrease in total protein and carbohydrate content of both diseased and healthy plants as compared to control. Diseased plants more adversely affected than healthy. Whereas substantial increase in total phenol was observed in both diseased and healthy plants. Among the amino acids proline, methionine, tyrosine and tryptophane were found in appreciable amount in diseased plants.

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Section: Methodsmentioning

confidence: 99%

Effects of Systemic Fungicides on Nutritive Composition of Diseased and Healthy Plants of Triticum aestivum L.

Siddiqui¹,

Ahmed²

2000

Pakistan J. of Biological Sciences

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“…A highly purified funSequence of peptides and proteins was analysed by the manual Edman degradation method [ 51. Identification of the phenylthiohydantoins was performed by silica gel thin-layer chromatography [6] and by back hydrolysis to parent amino acids [7]. Table 1 Amino acid compositions of amino-terminal CNBr-fragment CB-1, tryptic peptides (T-l -T-4) and a chymotryptic peptide CB-lC-3, corresponding to CB-1 …”

Section: Methodsmentioning

confidence: 99%

Sequence homology between barley trypsin inhibitor and wheat α‐amylase inhibitors

1982

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“…Samples (2 pl) were then chromatographed on thin-layer plates of silica gel G with ethanol/ water (70:30, by vol.) at room temperature (Brenner et al, 1965). The glutamate (Rp 0.60) migrated with little streaking, while the yellow-brown y-glutamyl hydroxamate (iron salt) remained near the origin.…”

Section: -2mentioning

confidence: 99%

Effects of D-Glutamate on Enzymes of Ammonia Assimilation in Bacillus megaterium NCIB 7581

White

1979

Journal of General Microbiology

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Enzymes possibly concerned in the assimilation of ammonia were assayed in Bacillus megaterium NCIB 7581 after growth with ammonium sulphate as sole source of nitrogen. Alanine dehydrogenase and aspartase were not detected, but both NADPH-dependent glutamate dehydrogenase and glutamate synthase (NADH-or NADPH-dependent) were found. Glutamine synthetase was also present, though differing methods of assay gave different values for its activity.Glutamate dehydrogenase was competitively inhibited by D-glutamate, whereas glutamate synthase was insensitive to D-glutamate or D-glutamine (singly or together). D-Glutamate was a substrate for glutamine synthetase, and the use of L-glutamate by this enzyme was partly inhibited by a 10-fold molar excess of D-glutamate. L-Glutamine strongly inhibited glutamine synthetase, but D-glutamine had no effect.A D-glutamate-resistant substrain (grown with ammonium sulphate as nitrogen source) contained 10 times more glutamate dehydrogenase activity than did the wild-type under the same conditions, and the enzyme showed altered affinity for 2-oxoglutarate and for Dglutamate. Activities of glutamate synthase and glutamine synthetase in the substrain were similar to those in the wild-type.Glutamate dehydrogenase was absent from organisms grown with nitrate as sole nitrogen source, yet growth under these conditions was still inhibited by D-glutamate. I N T R O D U C T I O NGrowth of Bacillus megaterium NCIB 7581 in a simple chemically defined medium was strongly inhibited by D-glutamate when ammonium sulphate was the nitrogen source (White, 1979). D-Glutamate was not inhibitory in the presence of L-glutamate or other L-amino acids that, like L-glutamate, could act as sole nitrogen sources for growth. DGlutamate might therefore inhibit the assimilation of ammonia by B. megaterium 758 1 and this paper describes a study of the enzymes (glutamate dehydrogenase, glutamate synthase, glutamine synthetase, aspartase and alanine dehydrogenase) that might take part in this process. The effect of D-glutamate on transaminases that use L-glutamate as substrate was also examined. METHODSOrganisms. BuciZlus megaterium NCIB 7581 and 758 1 GRA-1 (a D-glutamate-resistant substrain) were described by White (1979); 7581 GRN-1 (another D-glutamate-resistant substrain) is described in this paper. Escherichiu coli W (ATCC 9637) was described by White (1976). This organism was used to provide an extract with high enzymic activity to check the proper functioning of the assays for glutamine synthetase (four methods) and glutaminase.Media. Medium A1 (supplemented with biotin and citrate) was described by White (1979). When NaNO, (3 g 1-l) was used as the sole nitrogen source, (NH4),S04 was omitted from medium A1 and Na2S04. 10HzO 0022-1287/79/oooO-8123 $02.00 0 1979 SGM I1M I C 114

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Amino Acids and Derivatives

Cited by 72 publications

References 172 publications

Effects of Systemic Fungicides on Nutritive Composition of Diseased and Healthy Plants of Triticum aestivum L.

Effects of Systemic Fungicides on Nutritive Composition of Diseased and Healthy Plants of Triticum aestivum L.

Sequence homology between barley trypsin inhibitor and wheat α‐amylase inhibitors

Effects of D-Glutamate on Enzymes of Ammonia Assimilation in Bacillus megaterium NCIB 7581

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