SrasV1, Ncbi, Merge, bibRecord, 002709

A sorghum xylanase inhibitor-like protein with highly potent antifungal, antitumor and HIV-1 reverse transcriptase inhibitory activities.

Identifieur interne : 002709 ( Ncbi/Merge ); précédent : 002708; suivant : 002710

A sorghum xylanase inhibitor-like protein with highly potent antifungal, antitumor and HIV-1 reverse transcriptase inhibitory activities.

Auteurs : Peng Lin [République populaire de Chine] ; Jack Ho Wong ; Tzi Bun Ng ; Vincent Sai Man Ho ; Lixin Xia

Source :

Food chemistry [ 1873-7072 ] ; 2013.

RBID : pubmed:23871041

Descripteurs français

English descriptors

KwdEn :
- Animals, Antifungal Agents (chemistry), Antifungal Agents (isolation & purification), Antifungal Agents (pharmacology), Antineoplastic Agents, Phytogenic (chemistry), Antineoplastic Agents, Phytogenic (isolation & purification), Antineoplastic Agents, Phytogenic (pharmacology), Cell Line, Tumor, Cell Proliferation (drug effects), Endo-1,4-beta Xylanases (antagonists & inhibitors), Endo-1,4-beta Xylanases (chemistry), Enzyme Inhibitors (chemistry), Enzyme Inhibitors (isolation & purification), Enzyme Inhibitors (pharmacology), Fungi (drug effects), HIV Reverse Transcriptase (antagonists & inhibitors), HIV Reverse Transcriptase (chemistry), Humans, Kinetics, Mice, Plant Proteins (chemistry), Plant Proteins (isolation & purification), Plant Proteins (pharmacology), Protein Stability, Seeds (chemistry), Sorghum (chemistry).
MESH :
- chemical , antagonists & inhibitors : Endo-1,4-beta Xylanases, HIV Reverse Transcriptase.
- chemical , chemistry : Antifungal Agents, Antineoplastic Agents, Phytogenic, Endo-1,4-beta Xylanases, Enzyme Inhibitors, HIV Reverse Transcriptase, Plant Proteins.
- chemical , isolation & purification : Antifungal Agents, Antineoplastic Agents, Phytogenic, Enzyme Inhibitors, Plant Proteins.
- chemical , pharmacology : Antifungal Agents, Antineoplastic Agents, Phytogenic, Enzyme Inhibitors, Plant Proteins.
- chemistry : Seeds, Sorghum.
- drug effects : Cell Proliferation, Fungi.
- Animals, Cell Line, Tumor, Humans, Kinetics, Mice, Protein Stability.

Abstract

A 25-kDa protein, with an N-terminal amino acid sequence homologous to that of xylanase inhibitor and designated as xylanase inbibitor-like protein (XILP) was purified from sorghum seeds. The isolation protocol consisted of affinity chromatography, ion exchange chromatography, and gel filtration. XILP inhibited mycelial growth in various phytopathogenic fungi. The antifungal activity was thermostable and pH-stable. XILP inhibited proliferation of various cancer cell lines but did not do so in human embryonic liver (WRL 68) cells. There was no mitogenic activity toward mouse splenocytes. XILP reduced the activity of HIV-1 reverse transcriptase with an IC50 of 11.1μM, but lacked inhibitory activity toward HIV-1 integrase and SARS coronavirus proteinase. In conclusion, sorghum XILP is thermostable and pH stable and exhibits potent antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities.

DOI: 10.1016/j.foodchem.2013.04.013
PubMed: 23871041

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 001166
to stream PubMed, to step Curation: 001166
to stream PubMed, to step Checkpoint: 001236

Links to Exploration step

pubmed:23871041

Le document en format XML

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<front><div type="abstract" xml:lang="en">A 25-kDa protein, with an N-terminal amino acid sequence homologous to that of xylanase inhibitor and designated as xylanase inbibitor-like protein (XILP) was purified from sorghum seeds. The isolation protocol consisted of affinity chromatography, ion exchange chromatography, and gel filtration. XILP inhibited mycelial growth in various phytopathogenic fungi. The antifungal activity was thermostable and pH-stable. XILP inhibited proliferation of various cancer cell lines but did not do so in human embryonic liver (WRL 68) cells. There was no mitogenic activity toward mouse splenocytes. XILP reduced the activity of HIV-1 reverse transcriptase with an IC50 of 11.1μM, but lacked inhibitory activity toward HIV-1 integrase and SARS coronavirus proteinase. In conclusion, sorghum XILP is thermostable and pH stable and exhibits potent antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities. </div>
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<Abstract><AbstractText>A 25-kDa protein, with an N-terminal amino acid sequence homologous to that of xylanase inhibitor and designated as xylanase inbibitor-like protein (XILP) was purified from sorghum seeds. The isolation protocol consisted of affinity chromatography, ion exchange chromatography, and gel filtration. XILP inhibited mycelial growth in various phytopathogenic fungi. The antifungal activity was thermostable and pH-stable. XILP inhibited proliferation of various cancer cell lines but did not do so in human embryonic liver (WRL 68) cells. There was no mitogenic activity toward mouse splenocytes. XILP reduced the activity of HIV-1 reverse transcriptase with an IC50 of 11.1μM, but lacked inhibitory activity toward HIV-1 integrase and SARS coronavirus proteinase. In conclusion, sorghum XILP is thermostable and pH stable and exhibits potent antifungal, antiproliferative, and HIV-1 reverse transcriptase inhibitory activities. </AbstractText>
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<affiliations><list><country><li>République populaire de Chine</li>
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A sorghum xylanase inhibitor-like protein with highly potent antifungal, antitumor and HIV-1 reverse transcriptase inhibitory activities.

A sorghum xylanase inhibitor-like protein with highly potent antifungal, antitumor and HIV-1 reverse transcriptase inhibitory activities.

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