Isolation of an Angiotensin I-Converting Enzyme Inhibitory Protein with Antihypertensive Effect in Spontaneously Hypertensive Rats from the Edible Wild Mushroom Leucopaxillus tricolor

Molecules. 2015 Jun 1;20(6):10141-53. doi: 10.3390/molecules200610141.

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 mg∙mL-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.

Keywords: ACE inhibitory protein; Leucopaxillus tricolor; inhibitory pattern; spontaneously hypertensive rat.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agaricales / chemistry
  • Amino Acid Sequence
  • Angiotensin-Converting Enzyme Inhibitors / chemistry
  • Angiotensin-Converting Enzyme Inhibitors / isolation & purification*
  • Angiotensin-Converting Enzyme Inhibitors / pharmacology
  • Animals
  • Antihypertensive Agents / chemistry
  • Antihypertensive Agents / isolation & purification*
  • Antihypertensive Agents / pharmacology
  • Binding, Competitive
  • Blood Pressure / drug effects
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Fruiting Bodies, Fungal / chemistry*
  • Fungal Proteins / chemistry
  • Fungal Proteins / isolation & purification*
  • Fungal Proteins / pharmacology
  • Hypertension / drug therapy*
  • Hypertension / metabolism
  • Hypertension / physiopathology
  • Male
  • Molecular Sequence Data
  • Molecular Weight
  • Peptidyl-Dipeptidase A / metabolism*
  • Protein Binding
  • Rats
  • Rats, Inbred SHR

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Antihypertensive Agents
  • Fungal Proteins
  • Peptidyl-Dipeptidase A