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1988 (1)
1Author    Thomas Vom Bruch, Klaus-Heinrich RöhmRequires cookie*
 Title    Fluorescence Properties of Hog Kidney Aminoacylase I  
 Abstract    The state of the tryptophan residues of porcine kidney aminoacylase I (EC 3.5.1.14) was investigated by fluorescence spectroscopy and chemical modification. The pH-dependence of the fluorescence emission spectrum of the enzyme indicates that its native conformation prevails between pH 6 and 9.5. Within this range, the ionization of a residue with an apparent pKa of 7.1 quenches the enzyme fluorescence by about 15%. A similar reduction of fluorescence intensity accompanies the inactivation of aminoacylase I by treatment with N-bromosuccinimide in low excess. This suggests that in both cases a single tryptophyl residue out of eight residues per subunit is affected. Quenching by iodide revealed that, in the native conformation of the enzyme, 5—6 tryptophans per subunit are accessible, while 2—3 are buried within the protein. 8-Anilinonaph-thalene-L-sulfonate (ANS) is tightly bound to aminoacylase I (1 mol/mol dimer, K d < 1 PM). ANS binding does not interfere with substrate turnover; the spectroscopic properties of the amino-acylase-ANS complex are consistent with bound ANS being excited by radiationless energy transfer (RET) from buried tryptophyl residues of the enzyme. 
  Reference    Z. Naturforsch. 43c, 671—678 (1988); received June 3 1988 
  Published    1988 
  Keywords    Aminoacylase, Kidney, Tryptophan, Fluorescence, ANS 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0671.pdf 
 Identifier    ZNC-1988-43c-0671 
 Volume    43