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Biomedical subjects

W P Herrmann

Publications and source records attributed to W P Herrmann.

At least 19 recordsLinked to original sources
PubMed1986

[Etiology of acrodermatitis chronica atrophicans and erythema chronicum migrans].

In Lyme's disease (LD) as well as in the European form of erythema chronicum migrans (ECM), the etiologic agents are spirochetes. As fas as we know by now, these microbes are closely related but not identical. Consequently, LD and ECM should be regarded as closely related but not as identical diseases. The sera of our 21 patients suffering from acrodermatitis chronica atrophicans (ACA) contained elevated antibody titers directed against the etiological agent found in ECM. These findings strongly suggest that ACA is also induced by spirochetes-possibly by the same microbes found in ECM.

Acrodermatitis↗
PubMed1979

[Necrotizing fascitis (author's transl)].

Necrotizing fasciitis is a rare and little known infectious disease of the skin with a mortality, despite modern antibiotic treatment, of 25--50%. A case of the disease in a 63-year-old woman is described. Treatment consisted of wide incision and drainage of the subcutaneous abscess, with regression of the clinical signs and symptoms. There has been no recurrence. Determination of the anti-DN-ase-B titre was of diagnostic value in this instance.

Antibodies, Antinuclear↗
PubMed1979

Sialyltransferase levels and sialic acid concentrations in sera of patients with malignant melanomas.

Serum levels of sialyltransferase and sialic acid were measured in patients with malignant melanomas (n = 49), healthy control persons (n = 20), and patients with non-malignant skin disorders (n = 30). Both parameters were found to be higher in malignant melanoma patients than in healthy control persons, but they were not significantly higher in melanoma patients than in patients with benign skin disorders, unless widespread dissemination of metastases had occurred. The highest values were measured in patients with liver and lung metastases. No general correlation was found between sialyltransferase activities and sialic acid concentrations. Sialic acid concentrations seem to be a better index for tumor spreading than sialyltransferase activities. In early stages of the disease, shedding from tumor cells is not the major source of elevated serum levels of sialyltransferase and sialic acid, respectively.

Adolescent↗
PubMed1979

Lymphocyte response to mitogens in patients with malignant melanoma.

Lymphocyte blast transformation of 23 melanoma patients was compared to that of 22 healthy persons after stimulation with the mitogens PHA, ConA, and PWM. Transformation rate of lymphocytes in microcultures was measured following 3H-Thymidin uptake in a Liquid-Scintillation-Counter. Calculations were based on analyses of variance. There was no significant difference in blastogenetic response between the 2 groups (patients and controls), but there were differences between the used mitogens.

Adolescent↗
PubMed1979

[How much of classical topical therapy is still current today? (author's transl)].

Classical topical therapy has been largely displaced by the development of up-to-date drugs and advances in the galenic field. Serious objections have even been leveled against some older drugs and others are no longer current in spite of their good efficacy (e.g. dyes) because less discriminatory drugs can be substituted for them. The fundamental principles of classical topical therapy are still as valid as ever (inherent action of the base). However, many of the active principles of the prechemotherapeutic era have meanwhile been superseded as for example boric acid, mercury, desquamative pastes, sulfur among others. In contrast to this, topical applications such as dithranol, salicylic acid, coal tar and a few others still belong to the permanent stock of dermatological topical therapy.

Administration, Topical↗
PubMed1976

Incomplete arylamidase in psoriasis scales.

Electrophoretic and immunological studies revealed that normal and pathologically altered epidermis contains an arylamidase with the electrophoretic mobility of an x-globulin. This enzyme seems to be immunologically identical with an arylamidase secreted by the prostate gland. In psoriasis scales the arylamidase migrates with the electrophoretic mobility of a beta-globulin. Presumably, this enzyme contains fewer neuraminic acid groups than the arylamidase of normal epidermis. It may well be that in psoriasis the synthesis of arylamidase is incomplete.

Aminopeptidases↗
PubMed1976

Immunological studies on the proteins of human eccrine sweat.

Proteins present in the eccrine sweat collected from the skin surface of male volunteers were studied. The protein content ranged from 0.154--0.774 g per liter. A total 2282 ml sweat was concentrated until a final protein content of 25 mg/ml was reached. Paper electrophoresis revealed 3 fractions migrating like alpha-, beta-, and gamma-globulins. Eight different proteins were demonstrated by immunoelectrophoretic analyses using rabbit antisera directed against human sweat proteins. Three of these proteins were identified as blood serum proteins. One of the remaining 5 proteins could be of epidermal origin; another one which occurs in comedones as well as in sweat seems to be eluted from the sebum film present on the skin surface.

Animals↗
PubMed1976

[Immunological demonstration of beta-glucuronidase in eccrine sweat (author's transl)].

Electrophoretic and immunological investigations on highly concentrated sweat have shown that human eccrine sweat contains 6 different esterases. Two of them were found to hydrolyze naphthol-AS-Bi-beta-D-glucuronide. One of the two glucuronic acid ester splitting enzymes is likely to be a substrate-specific beta-glucuronidase. The other one is a non-specific carboxyl-esterase occurring in numerous organs and glandular secretions. This non-specific enzyme of widespread distribution can be mistaken for beta-glucuronidase because it hydrolyzes glucuronic acid esters as well as other synthetic substrates.

Carboxylic Ester Hydrolases↗
PubMed1976

Demonstration of carbohydrate structures in malignant melanoma tyrosinase.

Electrophoretic studies on malignant melanoma extracts before and after treatment with neuraminidase revealed that tyrosinase is a glycoprotein containing N-acetyl-neuraminic acid. Double diffusion tests using Concanavalin A and the lectin from Ricinus communis show that the carbohydrated chain of tyrosinase contains D-mannose as a sugar unit located within the carbohydrate chain. The terminal neuraminic acid groups are linked to D-galactose. The enzymatic activity of tyrosinase is not inhibited by Concanavalin A.

Carbohydrates↗
PubMed1976

Carbohydrate moieties of human seminal plasma arylamidases.

Human seminal plasma contains two arylamidases that differ considerably with respect to their antigenic structures, molecular weights and electrophoretic mobilities. Both enzymes are glycoproteins with different carcohydrate moieties. With the aid of precipitating lectins, the faster migrating arylamidase I was found to possess a PHA receptor (beta-Gal-GNAc-(Man)2-GNAc) with terminal N-acetyl-neuraminic acid groups. The carbohydrate moiety of arylamidase II consists of at least 2 types of carbohydrate chains: A disaccharide (beta-Gal(1-3)GalNAc) reacting with the lectin from Arachis hypogoea and in addition a chain containing the PHA receptor. This chain probably contains a terminal neuraminic acid group and a terminal fucosly group.

Aminopeptidases↗
PubMed1976

Immunological demonstration of multiple esterases in human eccrine sweat.

Eccrine sweat collected from the human skin surface contains at least five different esterases. One of them is a cholinesterase. A non-specific carboxylesterase with the electrophoretic mobility of an alpha-globulin appears to be a serum protein. Besides this, there are two isoenzymes of human origin migrating with the same electrophoretic mobility as gamma-globulins. These two isoenzymes are immunologically identical with a non-specific carboxylesterase occurring in numerous organs and body fluids. Lipase activity could not be demonstrated.

Carboxylic Ester Hydrolases↗