Abstract:
:Intracellular aminopeptidase synthesized by a soil strain of Pseudomonas sp. was purified 323-fold using the following procedure: saturation with ammonium sulfate, separation by preparative electrophoresis, anion-exchange chromatography and gel filtration chromatography. Molecular weight of the enzyme determined according to the latter method was 57 kDa. Aminopeptidase showed a high substrate specificity and affinity to Phe-beta-naphtylamide (Phe-beta-NA) as a substrate. A considerable inhibition of the enzymatic activity by iodoacetamide and p-chloromercuribenzoate (p-CMB) led to the conclusion that it was a cysteine aminopeptidase. Hydrosulphide compounds markedly stabilised the enzyme. Ethylenediaminetetra-acetic acid (EDTA), a metalloenzyme inhibitor, caused a double increase in the phenylalanyl aminopeptidase activity.( )Mg(2+) ions activated the enzyme to a negligible extent, whereas Co(2+), Cu(2+), Cd(2+) and Pb(2+) ions contributed to its inhibition. The highest enzymatic activity was observed at 37 degrees C and pH 7.0.
journal_name
J Basic Microbioljournal_title
Journal of basic microbiologyauthors
Jankiewicz U,Bielawski Wdoi
10.1002/1521-4028(200208)42:4<260::AID-JOBM260>3.0subject
Has Abstractpub_date
2002-01-01 00:00:00pages
260-7issue
4eissn
0233-111Xissn
1521-4028journal_volume
42pub_type
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