Transamidinase of hog kidney. IV. Effect of dinitrophenylation.
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Biomedical subjects
Publications and source records attributed to E Grazi.
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A review of the literature concerning "treadmilling" and fragmentation of actin filaments indicates that these two processes take place under similar conditions and that the mere difference of critical concentration at the two ends of the actin filaments is not a sufficient prerequisite for the exchange of actin monomers with polymer subunits. The hypothesis is made that fragmentation is the main prerequisite for the exchange. A repair mechanism for actin filaments is also presented.
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The existence of a 5'-nucleotidase has been demonstrated in human blood platelets. The enzyme has a low Km (20 microM) for adenosine monophosphate. It is prevalently located on the external surface of the plasma membrane as demonstrated by the similar degradation of exogenous AMP by intact and lysed platelets. Also results of inactivation studies by means of non penetrating chemical reagents point to this conclusion. Activity is inhibited by glucosyl moieties specific lectins (e.g. Concanavalin A) with varying sensitivity in intact platelets, isolated membranes and in the solubilized form. Also micromolar concentrations of ADP inhibit the activity, possibly with a competitive pattern since this effect is much more evident at low substrate concentrations. On the basis of these results, it is suggested that this enzyme is involved in in loco adenosine production in the platelets, a process which can assume a physiological important role.