Decreased elastase activity in circulating granulocytes of systemic sclerosis patients: a possible pathogenetic role.
Explore the source record for details and available documents.
Blotting, Western↗
Biomedical subjects
G Cercignani
Publications and source records attributed to G Cercignani.
Critical parameters for the determination of aminopyrine demethylase (ADP) activity, as assayed in hepatic microsomes from mice and rats [proceedings].
Explore the source record for details and available documents.
Aminopyrine N-Demethylase↗
Enzymatic synthesis of purine 2'-deoxyriboside and its properties as an inhibitor of adenosine deaminases from calf intestinal mucosa and Bacillus cereus.
Enzymatic synthesis of purine 2'-deoxyriboside was obtained by reacting purine with excess 2-deoxy-alpha-D-ribose-1-phosphate in the presence of commercial bovine nucleoside phosphorylase; the product was isolated by semipreparative reverse phase HPLC with an overall 62% yield. Purine 2'-deoxyriboside was shown to behave as a competitive inhibitor of adenosine deaminase from calf intestinal mucosa and Bacillus cereus, with apparent Ki values of 4.5 and 8.5 microM, respectively.
Adenosine Deaminase Inhibitors↗
Substrate specificities of adenosine deaminase and adenosine phosphorylase from Bacillus cereus.
The substrate specificity of two adenosine metabolizing enzymes from Bacillus cereus has been investigated, using partially purified preparations. Adenosine deaminase is shown to be highly specific for adenosine (Km = 5.6 X 10(-5) M at pH 8.1); 2'-deoxyadenosine, formycin A and 2-amino-adenosine are deaminated by the enzyme preparation, but reaction rates are at least 20 times lower than that for adenosine at concentrations up to 0.1 mM, due to higher Km and/or lower Vmax values. 3'-deoxyadenosine is not attacked. Adenosine phosphorylase, on the other hand, can readily act on adenosine, 2'-deoxyadenosine, 2-amino-adenosine and N6-monoalkyl-adenosines; again, 3'-deoxyadenosine shows no appreciable activity as a substrate. The results obtained are briefly discussed, in relation also to current investigations on purine metabolism in vegetative forms and spores of B. cereus.
Adenosine Deaminase↗