daucus carota/protease

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Proteolytic and partial sequencing studies of the bifunctional dihydrofolate reductase-thymidylate synthase from Daucus carota.

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The bifunctional dihydrofolate reductase-thymidylate synthase (DHFR-TS) of Daucus carota has been further characterized as regards molecular weight, amino acid composition, protease digestion and microsequencing of proteolytic peptides. Data reported in this paper demonstrate that the carrot protein

Microbiome of root vegetables-a source of gluten-degrading bacteria

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Gluten is a cereal protein that is incompletely digested by human proteolytic enzymes that create immunogenic peptides that accumulate in the gastrointestinal tract (GIT). Although both environmental and human bacteria have been shown to expedite gluten hydrolysis, gluten intolerance is a growing

Partial amino-acid sequence of ECP31, a carrot embryogenic-cell protein, and enhancement of its accumulation by abscisic acid in somatic embryos.

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ECP31, an embryogenic-cell protein from carrot (Daucus carota L.), was purified by sequential column-chromatographic steps and digested by V8 protease on a nitrocellulose membrane. The resultant peptides were separated by reverse-phased column chromatography and sequenced. The sequences obtained

Purification of a trypsin inhibitor secreted by embryogenic carrot cells.

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A protease inhibitor with a molecular weight of about 12,800 was purified to electrophoretic homogeneity from Daucus carota cells. The protease inhibitor was heat stable and inhibited trypsin but had no activity toward chymotrypsin or subtilisin. Nonembryogenic as well as embryogenic strains

cDNA cloning of an extracellular dermal glycoprotein of carrot and its expression in response to wounding.

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Suspension-cultured cells of carrot (Daucus carota L.) synthesize and secrete a glycoprotein that is normally found only in dermal tissues (epidermis, endodermis and periderm). This protein, previously called GP57, is now referred to as EDGP (E xtracellular D ermal G lyco P rotein). We purified

Rapid Changes in Plasma Membrane Protein Phosphorylation during Initiation of Cell Wall Digestion.

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Plasma membrane vesicles from wild carrot cells grown in suspension culture were isolated by aqueous two-phase partitioning, and ATP-dependent phosphorylation was measured with [gamma-(32)P]ATP in the presence and absence of calcium. Treatment of the carrot cells with the cell wall digestion

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