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selaginella trichoclada/dl proline

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LidwoordKlinische proevenOctrooien
6 resultaten
Drought is one of the most severe limitations to plant growth and productivity. Resurrection plants have evolved a unique capability to tolerate desiccation in vegetative tissues. Fern-ally Selaginella tamariscina (Beauv.) is one of the most primitive vascular resurrection plants, which can survive

Trehalose 6-phosphate synthase from Selaginella lepidophylla: purification and properties.

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A protein of 440 kDa with trehalose 6-phosphate synthase activity was purified with only one purification step by immobilized metal affinity chromatography, from fully hydrated Selaginella lepidophylla plants. The enzyme was purified 50-fold with a yield of 89% and a specific activity of 7.05 U/mg
The biochemical changes in two Selaginella species namely, S. tamariscina (Beauv.) Spring and S. plana (Desv. ex Poir.) Heiron., as induced by desiccation and subsequent rehydration were explored. Plants were allowed to dehydrate naturally by withholding irrigation until shoot's relative water

Desiccation-induced physiological and biochemical changes in resurrection plant, Selaginella bryopteris.

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Selaginella bryopteris is a lycophyte resurrection plant, which incurves during desiccation and recovers on availability of moisture. The aim of the study was to test and understand the various physiological and biochemical changes the fronds undergo during desiccation and rehydration, to get an

Bioinformatic Identification and Analysis of Extensins in the Plant Kingdom.

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Extensins (EXTs) are a family of plant cell wall hydroxyproline-rich glycoproteins (HRGPs) that are implicated to play important roles in plant growth, development, and defense. Structurally, EXTs are characterized by the repeated occurrence of serine (Ser) followed by three to five prolines (Pro)
Lipid bodies store oils in the form of triacylglycerols. Oleosin, caleosin and steroleosin are unique proteins localized on the surface of lipid bodies in seed plants. This study has identified genes encoding lipid body proteins oleosin, caleosin and steroleosin in the genomes of five plants:
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