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W Wende

Publications and source records attributed to W Wende.

46 records · Page 3Linked to original sources
PubMedDate not supplied

Reduction of the size of acute, experimental myocardial infarction by Verapamil.

The effect of 0.1 mg/kg Verapamil on the extent of the ischemic area following ligation of a branch of the left descending coronary artery was studied in anesthetized open chest dogs. The sum of the ST-segment elevation during the entire period of occlusion in the epicardial ECG was 15 mV in control infarction compared to 9 mV (p smaller than 0.0005) when Verapamil was infused after ligation. Mean flow in the left descending coronary artery was reduced by coronary ligation alone on the average by 23%, but augmented by Verapamil for 5% above pre-occlusion control flow. Corresponding to the rise in the coronary flow and the drop in perfusion pressure under the influence of Verapamil, the increase of left coronary artery resistance induced by coronary occlusion was diminished. The positive effect of Verapamil on the size of myocardial infarction as estimated from the epicardial ST-segment changes is probably not induced by coronary vasodilatation, but by the Ca-antagonizing effect of this drug, as described by other authors.

Acute Disease↗
PubMedDate not supplied

The mechanism of DNA cleavage by the type II restriction enzyme EcoRV: Asp36 is not directly involved in DNA cleavage but serves to couple indirect readout to catalysis.

Three different mechanisms have been proposed to describe DNA cleavage by the type II restriction endonuclease EcoRV, which differ in the number and function of metal ions directly involved in catalysis and the different roles assigned to amino acid residues in the active sites and a phosphate group of the substrate. There are only four acidic amino acid residues close to the scissile bond: the essential Asp74 and Asp90, the non-essential Glu45, and Asp36. We show here that Asp36 can be exchanged for alanine, with only minor effects on the cleavage rate of the nearby phosphodiester bond, excluding that Asp36 could be directly involved in catalysis. Hence, the two versions of the two-metal-ion mechanism are not compatible with the experimental data, because too few ligands for two metal ions are present near the active site of EcoRV. Our result, thus, supports the one-metal-ion mechanism for EcoRV. We suggest that Asp36 has an allosteric effect by which specific contacts between one strand of the DNA and one subunit of the enzyme trigger the activation of one catalytic center. Given the similar structures of the active sites of EcoRV, EcoRI, BamHI, PvuII and FokI, as well as the occurrence of a characteristic catalytic motif in several other restriction enzymes, we conclude that these enzymes most likely share a similar mechanism of DNA cleavage, whose characteristic feature is the involvement of only one Mg2+ ion in catalysis.

Aspartic Acid↗