A hydrophobic site on the surface of the angiotensin-converting enzyme molecule

Using the hydrophobic fluorescent dye 8-anilino-1-naphthalenesulfonic acid (8-ANS), a hydrophobic site on the surface of the protein globule of angiotensin-converting enzyme (ACE) from bovine lung was found. The dissociation constant of the ACE-8-ANS complex was estimated as 1.5 +/- 0.2 microM. This...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Biochemistry (Moscow) 2002-05, Vol.67 (5), p.553-557
Hauptverfasser:	Voronov, S V, Skirgello, O E, Troshina, N N, Orlova, M A, Kost, O A
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino acids Anilino Naphthalenesulfonates Animals Binding Sites Catalysis Cattle Complexation Dissociation Dyes Enzyme kinetics Enzymes Fluorescence Fluorescent Dyes Gamma Rays Hydrophobic and Hydrophilic Interactions Hydrophobicity Irradiation Lung - enzymology Octoxynol Organic acids Peptidyl-Dipeptidase A - chemistry Peptidyl-Dipeptidase A - metabolism Protein Conformation - radiation effects Proteins Rate constants Surface Properties Thermodynamics Water
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	Using the hydrophobic fluorescent dye 8-anilino-1-naphthalenesulfonic acid (8-ANS), a hydrophobic site on the surface of the protein globule of angiotensin-converting enzyme (ACE) from bovine lung was found. The dissociation constant of the ACE-8-ANS complex was estimated as 1.5 +/- 0.2 microM. This hydrophobic site is far from the ACE catalytic sites because the binding of the hydrophobic dye does not influence ACE activity. Shielding of the ACE hydrophobic site due to the complex formation with 8-ANS or Triton X-100 resulted in pronounced stabilization of the enzyme against the action of water radiolysis products during gamma-irradiation of dilute solutions of ACE.
ISSN:	0006-2979 1608-3040
DOI:	10.1023/A:1015598228545