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E Junger

Publications and source records attributed to E Junger.

3 recordsLinked to original sources

Binding and degradation of insulin by plasma membranes from bovine liver isolated by a large scale preparation.

With the large-scale preparation described, as much as 1 kg of bovine liver can be processed, giving a yield of more than 1 g plasma membrane protein. From analytical and morphological criteria the plasma membrane fraction isolated mainly derives from bile-canalicular and contiguous areas of the hepatocytes. The insulin binding activity is quite similar to insulin receptors in other cell systems and membrane preparations. Insulin-degrading activity is very low in the isolated plasma fraction. Most of degrading activity is located in a microsomal membrane fraction. Nevertheless the Km and the pH dependence of the insulin-degrading activity in both fractions are nearly identical. From these studies we conclude that binding and degradation of insulin are two independent processes located on different cell organelles.

Animals

Quantitative autoradiographic light- and electron microscopic studies on the retinohypothalamic connections in the rat.

Light microscopic autoradiography performed subsequent to intraocular injection of 3H-leucine revealed silver grains (SG) above axons of the optic tract which could be followed into the ventral and caudal portion of the suprachiasmatic nuclei (SCN) and above the contralateral anterior hypothalamic nucleus (AHN). By high resolution photometric measurement and computer processing the labelled areas were analysed, thus yielding statistical data of the relative grain distribution. The highest SG density was found in the ventrolateral part of both SCN (SCvl), confirming earlier reports concerning retinohypothalamic connections. That area exhibiting a cytoarchitecture different from the remaining nucleus was traversed, however, by numerous labelled axons. In the caudal part of both SCN a specific projection field of retinal fibres could be located. Here, almost no traversing fibres contribute to the rather circumscribed marked area. In the ventral part of the contralateral AHN, diffuse labelling well above background levels could be observed. Distinction between bypassing and terminating fibres within the SCvl could not be made using light microscopy. Analysis of SG distribution of the SCvl with electron microscopic autoradiography revealed a specific localization of SG within presynaptic terminals containing clear vesicles and pale mitochondria.

Animals

Structure of pyruvate dehydrogenase complex. Comparison between freeze-etching and negative staining.

Pyruvate dehydrogenase complex (pyruvate : lipoate oxidoreductase (decarboxylating and acceptor-acetylating), EC 1.2.4.1), from pig heart, was studied by spray freeze etching and negative staining. From freeze etching experiments an average particle weight of 7-10(6) was estimated. Negative staining after glutaraldehyde fixation and freeze etching of unfixed and prefixed enzyme solutions yielded no significant difference in particle dimensions: the majority of the isometric complex molecules measured approximately 400 A in diameter. Tantalum tungsten shadowed freeze etch replicas indicated that the surface of the complex is built up of globular units. The relative positions of these units are in good agreement with the model still under discussion.

Animals