Two different gamma-glutamyltransferases during development of liver and small intestine: a fetal (sialo-) and an adult (asialo-) glycoprotein.
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Biomedical subjects
Publications and source records attributed to W Gerok.
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In this investigation a new possibility of isoenzyme-differentiation of the gamma-glutamyl-transferase (GGT) (EC Nr.2.3.2.2.) was demonstrated by Concanavalin A and Con A-Sepharose. Because of the different sugar content of the glycoproteins distinction between liver- and kidney-GGT is possible. Furthermore it was possible for the first time to show a different precipitation behaviour of one glycoprotein to Concanavalin A in certain diseases. In cases of alcoholic hepatitis GGT looses its Concanavalin A-affinity because of increased neuraminic acid concentration. The possible reasons of the different behaviour to the binding affinity of Con A and Con A-Sepharose and GGT as well as additional use for enzyme-differentiation by Con A-Sepharose affinity chromatography are discussed.
In two patients intrahepatic cholestasis and cholestatic liver disease probably due to N-propyl ajmaline were observed. In both cases there was a four-week-interval between the first ingestion of the drug and the onset of jaundice. In one case with rigors there was a temporary rise in temperature and cholestasis. In the other there was a two to three week prodromal period of pruritus and gastro-intestinal symptoms. Both cases were characterised by blood and pronounced tissue eosinophilia in the periportal zones, a marked increase of cholestatic and hepatic cell enzymes, serum bilirubin and cholesterol, a moderate increase in erythrocyte sedimentation rate and absence of leucocytosis. Pathological laboratory findings returned to normal spontaneously within 5 weeks in one case and within two weeks under steroid therapy in the other.
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Enzymes of extramitochondrial, mitochondrial and lysosomal origin were differentiated by the method of fractional tissue extraction from rat liver. It could be confirmed that soluble enzymes of the extramitochondrial (cytoplasmatic) compartment (glycerine aldehydphosphate-dehydrogenase, argininosuccinate lyase) and soluble enzymes of the mitochondrial matrix can be differentiated easily according to their different intracellular localisation. Additionally, our results emphasize that soluble enzymes of both compartements and marker-enzymes of the lysosomal cell space which are known to be structurally-bound, can be differentiated too. However, the method failed to establish significant differences between enzymes located in the submitochondrial compartment (adenylatekinase, monaminooxidase and succinic-dehydrogenase) and lysosomal enzymes (cathepsin-D and N-acetyl-D-glucosaminidase).
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Genetic information from the bacterium Escherichia coli was transferred to human cells by means of the specialized transducing phage lambda plac carrying the bacterial z gene for the enzyme beta-galactosidase (geta-D-galactoside galactohydrolase, EC 3.2.1.23). As recipient cells, cultured skin fibroblasts from a patient with generalized gangliosidosis (GMI-gangliosidosis Type I) characterized by a severe deficiency of beta-galactosidase activity were used. The deficient human cells were incubated with the bacteriophage lambda plac or lambda plac DNA and beta-galactosidase activity was measured in order to detect gene transfer and acceptance of the prokaryotic information in the mammalian system for transcription and translation. The expression of the phage genome in the deficient fibroblasts could be demonstrated by detection of higher beta-galactosidase activity after incubation with phage lambda plac in three out of 19 experiments and in four out of 16 experiments after treatment with lambda plac DNA. Lambda plac DNA induced much higher enzyme activities than infective phage particles. Immunochemical and physicochemical assays could not distinguish the induced beta-galactosidase activity from that of the z-gene product of E. coli.
1. Defects in transport systems of renal tubules are caused by partial tubular dysfunction without preceeding renal disease. There is a well delineated disturbance for the reabsorption of certain substances. Most commonly the defects in transport of renal tubules are genetically determined. 2. Symptoms are due to secondary renal dysfunction and nephrolithiasis or extrarenal disturbances. Primary defects in transport systems of renal tubules, therefore, should be considered for differential diagnosis. 3. There is no therapy for the genetic defect. However, in case of early detection a symptomatic treatment is mandatory. This prevents clinical symptoms and sequelae.