1.
Acta Biochim Biophys Hung
; 25(1-2): 93-9, 1990.
Article
in English
| MEDLINE
| ID: mdl-2130576
2.
Acta Biochim Biophys Hung
; 22(1): 67-74, 1987.
Article
in English
| MEDLINE
| ID: mdl-3124424
ABSTRACT
A study has been made on the hydrolytic action of porcine kidney aminoacylase I (EC 3.5.1.14.) upon electrically charged substrates containing ionic groups both in the acyl moiety and in the C-terminal amino acids. In all cases a decrease in reactivity was found. An attempt has been made to elucidate the nature of this action.
Subject(s)
Amidohydrolases/metabolism , Amino Acids/metabolism , Animals , Electrochemistry , Hydrolysis , Ions , Kidney/enzymology , Kinetics , Substrate Specificity , Swine
3.
Acta Biochim Biophys Acad Sci Hung
; 12(4): 399-402, 1977.
Article
in English
| MEDLINE
| ID: mdl-613717