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D Beer

Publications and source records attributed to D Beer.

4 recordsLinked to original sources

[Local infiltration thrombolysis of arterial occlusions with tissue plasminogen activator].

Only few reports deal with local low dose thrombolysis of peripheral arterial occlusions by the infiltration technique with recombinant human tissue plasminogen activator (rTPA). We report the treatment of 45 cases (38 patients, 13 times women and 32 times men, aged 33 to 86 years). The patients suffered from thrombotic occlusions of the femoropopliteal artery (n = 39), a femoro-popliteal PTFE bypass (n = 3), a femorocrural bypass graft (n = 2) or a popliteal embolus (n = 1). The thrombus was infiltrated with 2.5 mg rTPA/hour attenuated to 30 ml normal saline solution. In the mean 7.1 mg rTPA was given. The rate of recanalisation was 76% during the days the patient stayed in hospital. The rate of recanalisation was higher (88%) in 16 cases suffering from acute arterial occlusion (< 24 hours). Even in those cases with undetectable or absent peripheral arterial runoff, therapeutic success was achieved at 92%.

Adult

The binding of D-gluconohydroximo-1,5-lactone to glycogen phosphorylase. Kinetic, ultracentrifugation and crystallographic studies.

Combined kinetic, ultracentrifugation and X-ray-crystallographic studies have characterized the effect of the beta-glucosidase inhibitor gluconohydroximo-1,5-lactone on the catalytic and structural properties of glycogen phosphorylase. In the direction of glycogen synthesis, gluconohydroximo-1,5-lactone was found to competitively inhibit both the b (Ki 0.92 mM) and the alpha form of the enzyme (Ki 0.76 mM) with respect to glucose 1-phosphate in synergism with caffeine. In the direction of glycogen breakdown, gluconohydroximo-1,5-lactone was found to inhibit phosphorylase b in a non-competitive mode with respect to phosphate, and no synergism with caffeine could be demonstrated. Ultracentrifugation and crystallization experiments demonstrated that gluconohydroximo-1,5-lactone was able to induce dissociation of tetrameric phosphorylase alpha and stabilization of the dimeric T-state conformation. A crystallographic binding study with 100 mM-gluconohydroximo-1,5-lactone at 0.24 nm (2.4 A) resolution showed a major peak at the catalytic site, and no significant conformational changes were observed. Analysis of the electron-density map indicated that the ligand adopts a chair conformation. The results are discussed with reference to the ability of the catalytic site of the enzyme to distinguish between two or more conformations of the glucopyranose ring.

Amino Acid Sequence

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