aspartic acid/majs

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Aspartic acid as an internal CO2 reservoir in Zea mays: Effect of oxygen concentration and of far-red illumination.

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By placing leaf segments first in CO2 in the dark, then in pure nitrogen either in the dark and afterwards in the light or immediately in the light, the existence of internal CO2 pools which can be used for photosynthesis had been demonstrated. In Zea mays L. there are two such pools: one which in

Bacillus ciccensis sp. nov., isolated from maize (Zea mays L.) seeds.

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Two Gram-stain-positive bacterial strains, designated as 5L6T and 6L6, isolated from seeds of hybrid maize (Zea mays L., Jingke 968) were investigated using a polyphasic taxonomic approach. The cells were aerobic, motile, endospore-forming and rod-shaped. Phylogenetic analysis based on 16S rRNA gene

Aspartic-acid synthesis in C3 plants.

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In a previous study (Melzer and O'Leary, 1987, Plant Physiol. 84, 58-60), we used isotopic methods to show that a substantial fraction of protein-bound aspartic acid in tobacco is derived from anaplerotic synthesis via phosphoenolpyruvate (PEP) carboxylase. Similar studies in soybean (Glycine max

Metabolism of Proline, Glutamate, and Ornithine in Proline Mutant Root Tips of Zea mays (L.).

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In excised pro(1-1) mutant and corresponding normal type roots of Zea mays L. the uptake and interconversion of [(14)C]proline, [(14)C]glutamic acid, [(14)C]glutamine, and [(14)C]ornithine and their utilization for protein synthesis was measured with the intention of finding an explanation for the

Genotypic effects on the amino acid relationships in maize (Zea mays L.) pollen and style.

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The free amino acid content of the pollen grains and the style from three single cross hybrids (Wf9 x H55, Ky49 x Ky27, K64 x K55) and two inbred lines (Oh43, H55) was determined. No tyrosine was detected in the pollen grains of any genotype. Significant differences between pollen genotypes were

Biochemical composition of maize (Zea mays L.) pollen : I. Effects of the endosperm mutants, waxy (wx), shrunken (sh 2) and sugary (su 1) on the amino acid content and fatty acid distribution.

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Proline was the most abundant amino acid with a mean value of 186.28 μ moles/mg dry pollen. The other amino acids tested were below 33 μ moles/mg dry pollen. The mutant wx significantly increased aspartic acid, valine, histidine and an unknown but significantly decreased α aminobutyric acid. The

Biochemical composition of maize (Zea mays L.) pollen : III. Effects of allele X storage interactions at the waxy(wx), sugary (su 1) and shrunken (sh 2) loci on the amino acid content.

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Pollen grains containing either the Wx, wx, Su 1, su 1, Sh 2 or sh 2 alleles were stored at 0, 1, 2, 3, 4 and 5 days at 2 °C. After each storage period, a portion of pollen from each genotype was analyzed for free amino acid content. Over all genotypes, storage significantly altered the content of

Side chain-side chain interactions of arginine with tyrosine and aspartic acid in Arg/Gly/Tyr-rich domains within plant glycine-rich RNA binding proteins.

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Plant glycine-rich RNA-binding proteins (GRRBPs) contain a glycine-rich region at the C-terminus whose structure is quite unknown. The C-terminal glycine-rich part is interposed with arginine and tyrosine (arginine/glycine/tyrosine (RGY)-rich domain). Comparative sequence analysis of forty-one

Complementary DNA cloning and characterization of ferredoxin localized in bundle-sheath cells of maize leaves.

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In maize (Zea mays L.) two leaf-specific ferredoxin (Fd) isoproteins, Fd I and Fd II, are distributed differentially in mesophyll and bundle-sheath cells. A novel cDNA encoding the precursor of Fd II (pFD2) was isolated by heterologous hybridization using a cDNA for Fd I (pFD1) as a probe. The

Roles of amino acids, protein, and fiber in leaf-feeding resistance of corn to the fall armyworm.

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The free amino acids have been shown by isolational work and choice bioassays to be more important than all other factors evaluated in defining leaf-feeding resistance of corn (Zea mays L.) to fall armyworm (FAW) [(Spodoptera frugiperda J.E. Smith)] larvae. 6-MBOA (6-methoxybenzoxazolinone) and

Differential Regulation of Maize Homoserine Dehydrogenase under Physiological Conditions.

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Homoserine dehydrogenase is associated with the multibranched pathway of amino acid biosynthesis originating with aspartic acid. Like most of the related pathway enzymes, this enzyme is localized in chloroplasts. The activity and regulatory properties of the threonine-sensitive isozyme of homoserine

Heterogeneity of storage proteins in maize.

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The extensive charge heterogeneity of maize (Zea mays L.) zeins observed in isoelectric focusing (IEF) (about 15 bands with pI's in the pH range 6-9) has been found to be independent of extraction procedures or of endosperm development. Zeins do not stain for glycoproteins and exhibit only one

Partial purification and characterization of dihydrodipicolinic Acid reductase from maize.

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Dihydrodipicolinic acid reductase, an enzyme which catalyzes the pyridine nucleotide-linked reduction of dihydrodipicolinic acid to tetrahydrodipicolinic acid in the biosynthetic pathway leading to l-lysine, has been partially purified from maize (Zea mays cv Pioneer 3145) kernels. The crude maize

KDEL-Containing Auxin-Binding Protein Is Secreted to the Plasma Membrane and Cell Wall.

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The auxin-binding protein ABP1 has been postulated to mediate auxin-induced cellular changes associated with cell expansion. This protein contains the endoplasmic reticulum (ER) retention signal, the tetrapeptide lysine-aspartic acid-glutamic acid-leucine (KDEL), at its carboxy terminus, consistent

An amino-acid-grown maize cell line for use in investigating nitrate assimilation.

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Studies on uptake and assimilation of nitrate in plants are confounded by differences in cell function associated with anatomical features of roots as well as by problems inherent with growing plants without nitrate. To circumvent these problems, a Zea mays L. embryo cell line was grown in

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