K
K E Jørgensen
Researcher at Aarhus University
Publications - 23
Citations - 677
K E Jørgensen is an academic researcher from Aarhus University. The author has contributed to research in topics: Vesicle & Valinomycin. The author has an hindex of 15, co-authored 23 publications receiving 675 citations.
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Journal ArticleDOI
Epithelial glycoprotein-330 mediates endocytosis of plasminogen activator-plasminogen activator inhibitor type-1 complexes.
Søren K. Moestrup,Søren Nielsen,Peter A. Andreasen,K E Jørgensen,Anders Nykjaer,Hans Røigaard,Jørgen Gliemann,E. I. Christensen +7 more
TL;DR: The results establish an endocytotic function of gp330 and suggest that gp330 is an important component of the fibrinolytic system in gp330-containing epithelial as found in, for example, kidney and lung.
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Enzymatically active Ca2+ ATPase from sarcoplasmic reticulum membranes, solubilized by nonionic detergents. Role of lipid for aggregation of the protein.
TL;DR: The data indicate that any bonds between ATPase polypeptide chains are easily disrupted by detergent and that lipid also may play a role in mediating contact between individual polypePTide chains in the tetrameric or trimeric units.
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An efficient method for the isolation and separation of basolateral-membrane and luminal-membrane vesicles from rabbit kidney cortex.
TL;DR: Uptake studies showed that both adult and newborn rabbit luminal-membrane vesicles, in contrast with the basolateral- Membrane preparations, possess an Na+-dependent electrogenic transport system for L-proline.
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The functional unit of calcium-plus-magnesium-ion-dependent adenosine triphosphatase from sarcoplasmic reticulum. The aggregational state of the deoxycholate-solubilized protein in an enzymically active form.
TL;DR: It is concluded that the catalytic activity of monomeric ATPase retains most of the features of vesicular ATPase and that extensive oligomer formation in gel-chromatographic experiments in the presence of deoxycholate probably reflects processes taking place during inactivation and delipidation of the protein.
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The Multiligand α2‐Macroglobulin Receptor/Low Density Lipoprotein Receptor‐Related Protein (α2MR/LRP)
Jørgen Gliemann,Anders Nykjaer,Claus Munck Petersen,K E Jørgensen,Marit Nyholm Nielsen,Peter A. Andreasen,E. I. Christensen,Aivar Lookene,Gunilla Olivecrona,S K Moestrup +9 more
TL;DR: The fusion of separate lines of research has greatly helped in elucidating the function of the giant members of the low density lipoprotein (LDL) receptor (LDLR) supergene family as mentioned in this paper.