Isolation of an Angiotensin I-Converting Enzyme Inhibitory Protein with Antihypertensive Effect in Spontaneously Hypertensive Rats from the Edible Wild Mushroom Leucopaxillus tricolor.
Molecules
; 20(6): 10141-53, 2015 Jun 01.
Article
em En
| MEDLINE
| ID: mdl-26039337
ABSTRACT
An 86-kDa homodimeric angiotensin I-converting enzyme (ACE) inhibitory protein designated as LTP was isolated from fruit bodies of the mushroom Leucopaxillus tricolor. The isolation procedure involved ultrafiltration through a membrane with a molecular weight cutoff of 10-kDa, ion exchange chromatography on Q-Sepharose, and finally fast protein liquid chromatography-gel filtration on Superdex 75. LTP exhibited an IC50 value of 1.64 mgâmL-1 for its ACE inhibitory activity. The unique N-terminal amino acid sequence of LTP was disclosed by Edman degradation to be DGPTMHRQAVADFKQ. In addition, seven internal sequences of LTP were elucidated by liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. Results of the Lineweaver-Burk plot suggested that LTP competitively inhibited ACE. Both LTP and the water extract of L. tricolor exhibited a clear antihypertensive effect on spontaneously hypertensive rats.
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Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Fúngicas
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Inibidores da Enzima Conversora de Angiotensina
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Peptidil Dipeptidase A
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Carpóforos
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Hipertensão
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Anti-Hipertensivos
Limite:
Animals
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article