Biomedical subjects
Publications and source records attributed to W P Herrmann.
Histiocytomas display a remarkably strong proteolytic activity. Electrophoretic and immunological studies reveald that this proteolytic activity is due, at least partially, to the presence of an arylamidase, previously described as "aminopeptidase I". This enzyme has been identified in various tissues of ectodermal, mesodermal and entodermal origin.
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.
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.
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.
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.
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.
1. Human tyrosinase is a glycoprotein containing N-acetylneuraminic acid. 2. The terminal neuraminic acid groups are linked to D-galactose. 3. In addition, human tyrosinase reacts strongly with concanavalin A. This finding indicates that the carbohydrate chain of human tyrosinase contains D-mannose. 4. The data presented here suggest that the carbohydrate moiety of human tyrosinase is linked to the protein core in an alkali-stable form. 5. Alkali-labile carbohydrate chains which occur predominantly in membrane bound glycoproteins could not be demonstrated serologically.
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