agrostis castellana/cistein

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Copper stress-induced changes in leaf soluble proteome of Cu-sensitive and tolerant Agrostis capillaris L. populations.

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Changes in leaf soluble proteome were explored in 3-month-old plants of metallicolous (M) and nonmetallicolous (NM) Agrostis capillaris L. populations exposed to increasing Cu concentrations (1-50 μM) to investigate molecular mechanisms underlying plant responses to Cu excess and tolerance of M

Differential accumulation of soluble proteins in roots of metallicolous and nonmetallicolous populations of Agrostis capillaris L. exposed to Cu.

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Differential expression of soluble proteins was explored in roots of metallicolous (M) and non-M (NM) plants of Agrostis capillaris L. exposed to increasing Cu to partially identify molecular mechanisms underlying higher Cu tolerance in M plants. Plants were cultivated for 2 months on perlite with a

Candidate genes and molecular markers associated with heat tolerance in colonial Bentgrass.

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Elevated temperature is a major abiotic stress limiting the growth of cool-season grasses during the summer months. The objectives of this study were to determine the genetic variation in the expression patterns of selected genes involved in several major metabolic pathways regulating heat tolerance

Isolation and Partial Purification of Cadmium-Binding Protein from Roots of the Grass Agrostis gigantea.

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A cadmium-binding protein was isolated from roots of the grass Agrostis gigantea Roth. Heat-stable proteins were chromatographed on the anion exchanger QAE-Sephadex A-25. The major cadmium fraction was purified further by gel filtration on Sephadex G-75 in 1 molar KCl buffer. The resulting protein

Partial Purification and Characterization of Copper-binding Protein from Roots of Agrostis gigantea Roth.

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A Cu-binding protein was isolated from roots of the grass Agrostis gigantea Roth. Heat stable proteins were chromatographed on the strongly basic anion exchanger QAE-Sephadex A-25. Dark brown pigments were retained by the ion exchanger during elution of Cu-binding protein. Further purification was

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