Wiener klinische Wochenschrift
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Wien. Klin. Wochenschr. · Mar 1985
Randomized Controlled Trial Comparative Study Clinical Trial[Comparative study on the effect of diet, exercise and iodine balneotherapy on blood rheologic parameters in diabetics within the scope of a 4 week health resort stay in Bad Hall].
A total of 123 spa patients with inadequately controlled diabetes mellitus was divided into the following 3 therapeutic groups: 1. therapeutic exercise alone, 2. iodine therapy with iodine brine (including drinking cure with "iodine-brine concentrate"), 3. remedial exercise plus iodine brine therapy. All patients received a rigidly controlled diabetic diet. The following parameters were determined at the beginning and at the end of the cure: whole blood and plasma viscosity, fibrinogen, blood glucose, total and HDL-cholesterol, triglycerides, HbA1c, alpha 2-macroglobulin, total protein, microhaematocrit. ⋯ The largest decreases were shown by blood viscosity, relative viscosity, triglycerides, cholesterol and HbA1c in group III, and by plasma viscosity in group II. alpha 2-Macroglobulins did not change. Fibrinogen was raised in groups I and III. The importance of the improved blood rheological properties is discussed, particularly with respect to reduced erythrocyte flexibility in diabetics.
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Wien. Klin. Wochenschr. · Mar 1985
[Localization of functionally important areas of the regulator protein factor H using monoclonal antibodies].
Four monoclonal antibodies to the control protein of the complement system, factor H, were used to try to localize functionally important domains on the molecule. Attempts to inhibit the interaction of C3b and H in ELISA and agglutination assays by means of these monoclonal antibodies showed that two of them, namely MAH 1 and MAH 2, recognized an epitope in close proximity to the binding site for C3b on H. ⋯ The cofactor function of H with respect to C3b inactivator was inhibited by the same monoclonal antibodies which interfered with the binding of H to C3b. Since MAH 1, MAH 2, MAH 3 and MAH 4 all bind to the same tryptic 38 KD fragment of H, the binding site for C3b on H, as well as the cofactor activity seem to reside on this fragment.