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pinellia ternata/carbohydrate

Sábháiltear an nasc chuig an gearrthaisce
AiltTrialacha cliniciúlaPaitinní
7 torthaí

[Cation channels formed in lipid bilayer by Pinellia ternata lectin].

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú
Logáil Isteach / Cláraigh
Pinellia ternata lectin (PTL), a protein exhibiting hemagglutination activity and carbohydrate binding specificity to mannan was purified from rhizome of Pinellia ternata. In this work the actions of PTL on artificial lipid bilayer were investigated by means of the two-compartment system of Mueller

[Facilitatory effect of Pinellia ternata lectin on quantal release of acetylcholine from nerve terminals].

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú
Logáil Isteach / Cláraigh
Pinellia ternata lectin (PTL) extracted from the rhizome of Pinellia ternata Briet by porcine thyroglobulin-Sepharose 4B column exhibits hemagglutination activity and carbohydrate binding specificity for mannan. Here we reported the effects of PTL on the resting membrane potential of muscle fiber

[Genetic transformation of Pinellia ternata with Agrobacterium tumefaciens-mediated sHSP genes].

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú
Logáil Isteach / Cláraigh
OBJECTIVE To establish an efficient genetic transformation system of Pinellia ternata. METHODS With petioles from test-tube seedlings of P. ternata as explants, Agrobacterium tumefaciens mediation method was adopted to explore the effect of phenolic substances, A. tumefaciens's concentration,

Prokaryotic expression and bioactivity analysis of N-terminus domain of Pinellia ternata agglutinin using alkaline phosphatase signal peptide.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú
Logáil Isteach / Cláraigh
Pinellia ternata agglutinin (PTA) from the tubers of P. ternata is a two-domain monocot mannose-binding lectin. Pta-n encoding N-terminus domain of PTA (PTA-N) was fused with Escherichia coli alkaline phosphatase signal peptide (APSP) gene by polymerase chain reaction (PCR) for secretion expression.

Effects of Pinellia ternata (Thunb.) Berit. on the metabolomic profiles of placenta and amniotic fluid in pregnant rats.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú
Logáil Isteach / Cláraigh
BACKGROUND Banxia (BX) is the root of Pinellia ternata (Thunb.) Berit. Its processed products, such as Jiang Banxia (JBX), have been clinically used in traditional Chinese medicine to treat vomiting, coughing, and inflammation. However, data for their safety for pregnant women are contradictory and

cDNA cloning, characterization, and pharmacologic evaluation of anticancer activity of a lectin gene in Pinellia integrifolia.

Ní féidir ach le húsáideoirí cláraithe ailt a aistriú
Logáil Isteach / Cláraigh
Plant lectins are proteins that possess at least one non-catalytic domain, which could reversibly bind to specific monosaccharides or oligosaccharides. The important roles played by plant lectins in immune regulation, signaling pathways, and plant defense could be attributed to their specific
A comprehensive profiling method was established for the determination of various chemicals in Pinellia (P.) ternata and pedatisecta species. The profiling method comprises a fast ultrasonic extraction with various solvents, followed by GC-MS and LC-APCI-MS analysis. A total of 73 polar components
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