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Biomedical subjects

R Niedner

Publications and source records attributed to R Niedner.

At least 37 records · Page 2Linked to original sources
PubMed1988

[Transdermal therapeutic systems (TTS)].

The technique, pharmacokinetics, and advantages and disadvantages of transdermal drug delivery systems (TDS) are discussed. Special emphasis is laid on the dermatological problems arising during use of the TDS, such as irritation, sensitization, and the effects of occlusion, dermatoses, skin microflora and epidermal metabolism.

Administration, Cutaneous↗
PubMed1987

[Does the anesthesia method modify the results of dermatologic surgery of the nose?].

Since dermatosurgery has become a generally acknowledged subsection of dermatology, it seems strange that we have got so little account regarding the influences of anesthesia on the results of plastic surgery in the antrofacial region. A long-term follow-up of 139 patients, who had received regional flaps or free grafts because of tumors of the nose, revealed that the functional and esthetic results of operations carried out in local anesthesia were perfectly comparable with those in general anesthesia. We recommend local anesthesia because of its easy handling and little complications even in elderly polymorbid patients.

Anesthesia, General↗
PubMed1986

[Effect of zinc on wound healing].

Topical application of zinc sulfate 0.5% leads to improvement of the healing process: In comparison to controls, the granulation tissue is constructed more systematically, the formation of collagen is more advanced, and its amount is increased.

Administration, Topical↗
PubMed1985

[Idiopathic progressive atrophoderma of Pasini-Pierini with the presence of antinuclear antibodies].

Atrophodermia idiopathica progressiva Pasini-Pierini (AIPP) in two young female patients is described. This disease, which begins in the second decade, is slowly progressive and has the characteristics of an originally atrophic dermatosis. No regression to sclerosised lesions could be observed. The distribution of lesions was a strictly one-sided, with the radicular pattern of some lesions suggesting the participation of neurogenic factors. The finding of antinuclear antibodies of the nucleolar type suggests an immunological pathogenesis. HLA typing did not reveal any extraordinary patterns or, interestingly, any of the types associated with immunological diseases.

Adult↗
PubMed1975

[The reciprocal actions of phenprocoumon (Marcumar) with human serum albumin, erythrocytes and blood].

The binding properties of phenprocoumon (PhC) to human serum albumin (HSA) and to red blood cells (RBC) were determined by using the equilibrium dialysis. Analysis of PhC-binding data to HSA at pH 7.4 and temperatures of 10 degrees C and 27 degrees C resulted in binding constants (k) of 11.8 - 10(4) and 7.0 - 10(4), in free standard enthalpy changes deltaG0 of -6.658 and -6.651 kcal/mol, and in standard enthalpy change TdeltaS0 of 1.386 and 1.469 kcal/mole, respectively. The standard enthalpy change deltaH0 was -5.182 kcal/mole for both temperatures. These results indicate that the binding between PhC and HSA is predominantly effected by hydrophobic interactions. At pH 7.4 the binding to HSA is essentially characeterized by two straight lines of binding, whereas at pH 9 and 10 there are three. With increasing pH more binding sites become free and the affinity of PhC to HSA grows. Studies of binding properties to RBC indicate a strong binding of PhC to hemoglobin (k 7.9 - 10(5)), but only a weak one to red cell membranes (binding ratio hemoglobin to ghosts 66 : 1). In a combined system of HSA and RBC, competition occurs between both components and therefore the strength of binding decreases. At therapeutic PhC-concentrations, 91.7% of the PhC are bound to the whole blood, 20.8% to RBC, and 70.9% to HSA. With increasing concentrations of PhC the binding to RBC declines to 10.5% accompanied by an approximately unchanged binding to whole blood of 92.1%; whereas binding to HSA increases to 81.6%. The affinity of PhC to HSA grows larger than its affinity to RBC. The total binding to blood remains unchanged within a 21-fold range and it is predominantly determined by the affinity of HSA to PhC.

Blood↗
PubMed1975

[Rodenticidal action of warfarin/4th communication: Binding to serum albumin of mice and rats (author's transl)].

The binding properties of 3-(1'-phenyl-2'-acetylethyl)-4-hydroxycoumarine (warfarin-Na) to serum albumin of mice and rats were determined by using the equilibrium dialysis. The binding percentage (beta), the binding capacity (K), and the association constant (K1) were calculated. The results are characteristic for a strong binding of warfarin to serum albumin of rats but only a small one to serum albumin of mice, caused probably by the different albumin structures of these species.

Animals↗