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J Krause

Publications and source records attributed to J Krause.

At least 91 records · Page 5Linked to original sources
PubMed1987

Porin pores of mitochondrial outer membranes from high and low eukaryotic cells: biochemical and biophysical characterization.

The mitochondrial porins from mammalian tissues and from low eukaryotic cells were purified with a high yield, and their biochemical and functional properties were investigated. When analyzed by SDS gel electrophoresis, all mammalian porins show a very similar apparent molecular mass (35-35.5 kDa). In contrast yeast and Paramecium porins have a molecular mass of 30 and 37 kDa, respectively. The peptide maps of mammalian porins are very similar although small differences are apparent between porins of different tissues of the same organism and also between those of the same tissue of different organisms. The peptide patterns of porins from yeast and Paramecium are completely different from those of mammalian porins. Antibodies raised against the rat liver porin cross-react with all the other mammalian porins but not with that of yeast. The incorporation of porins into artificial lipid bilayer membranes showed that they are able to form pores with approximately the same specific activity. The single-channel conductance is for all porins, except for that of Paramecium, about 4 nS in 1 M KCl, corresponding to an effective pore diameter of 1.7 nm. They are voltage-dependent and switch to substates at transmembrane potentials higher than 10 mV. The number of gating charges varies, however, for pores from different tissues, indicating a different sensitivity to the potential as a result of a possible different function.

Adenosine Triphosphate↗
PubMed1986

Enrichment and biochemical characterization of boundary membrane contact sites from rat-liver mitochondria.

A subfraction of mitochondrial membranes was prepared from osmotically lysed rat liver mitochondria by density gradient centrifugation which contained the inner boundary membrane and the contact sites between this membrane and the outer membrane. The fraction was composed of inner and outer limiting membrane components as shown by the presence of specific marker enzymes, monoamine oxidase and glycerolphosphate oxidase. Surface proteolysis analysis, studies of cytochrome c permeability, and electron microscopy revealed the localization of the inner membrane component within a right-side-out outer membrane vesicle. Moreover, the outer membrane component in this fraction exhibited a higher capacity to bind hexokinase and had a higher specific activity of glutathione transferase than the pure outer membrane. In freeze-fracture analyses the fraction showed fracture plane deflections which may be specific for hydrophobic interactions between the two membranes.

Animals↗
PubMed1986

Cross-linking analysis of yeast mitochondrial outer membrane.

By enrichment of contact sites between the two mitochondrial boundary membranes it has been shown that this fraction contained a high activity of glutathione transferase and hexokinase which was bound to the outer membrane pore protein (Ohlendieck, K. et al. (1986) Biochim. Biophys. Acta 860, 672-689). Therefore, an interaction between the three proteins in the contact sites has been suggested. Cross-linking experiments with isolated outer membrane of yeast mitochondria show that glutathione transferase and the pore protein are already associated in the free outer membrane. Porin appeared to adopt four different oligomeric complexes in the membrane, including interactions with a 14 kDa polypeptide, which has glutathione transferase activity. The latter polypeptide could be phosphorylated by intrinsic or extrinsic protein kinases, while the porin itself was not phosphorylated. Yeast hexokinase, when bound to the outer membrane, was able to cross-link to the pore protein.

Cell Membrane↗
PubMed1985

[Experiences with Reflolux in blood sugar self testing].

As to correctness and accuracy the Reflolux system is comparable to the conventional measurement of blood glucose under laboratory conditions. Its handling is simple and safe so that diabetic patients are able to check their blood sugar reliably by self-control. Skilled patients achieve just as good results as laboratory personnel.

Blood Glucose↗
PubMed1984

Alterations in liver mitochondrial function as a result of fasting and exhaustive exercise.

The effect of exercise upon liver mitochondria structure and function was examined in fasted and fed rats, following a single run to exhaustion on a motor-driven treadmill. Exercise alone and exercise coupled with fasting both produced a significant decrease in the amount of hexokinase bound to the mitochondria, as well as reduction in the ADP/O ratio and acceptor control index measured in the presence of succinate. The mitochondria of the exercised animals, when exposed to freeze-fracture analysis while in state 3, displayed fewer deflections in the fracture plane between the inner and outer membrane than those isolated from control animals. This suggests that fewer contacts existed between the two membranes. Measurements based upon the binding of 8-anilinonaphthalene 1-sulphonate indicated that there was an increase in the net negative charge on the surface of the mitochondrial membranes of the exercised animals. All of these effects could be mimicked by incubation of mitochondria from control animals with free fatty acids. This fact, coupled with the observation that washing of the mitochondria with a solution comprising 5% (w/v) albumin could reverse all of the consequences of exercise, suggests that these alterations in mitochondrial structure and function may be the result of the increase in plasma free fatty acids that accompanies long-term exercise. Furthermore, the observation that the exercise-induced changes are dynamic and readily reversible indicates that the mitochondria were not necessarily damaged, but rather that the coupling of oxidative phosphorylation may be subject to physiological regulation.

Anilino Naphthalenesulfonates↗
PubMed1983

The binding of glycerol kinase to the outer membrane of rat liver mitochondria: its importance in metabolic regulation.

Glycerol kinase was found to associate with the hexokinase binding protein. The binding of glycerol kinase has a high specificity as illustrated by the fact that the magnitude of binding was reduced by glycerophosphate and antibodies against the hexokinase binding protein. A possible function of glycerol kinase binding to the mitochondria with respect to metabolic regulation is proposed for the following reasons: (i) Glycerol kinase seems to bind to the same binding protein as hexokinase. (ii) Both kinases were observed to be reversibly bound to the mitochondria in different metabolic situations, i.e., 10% of total cellular activity from both kinases is bound in starved rats whereas no activity of glycerol kinase and 30% of hexokinase become bound in fed rats. (iii) The kinetic properties of the associated glycerol kinase change in an analogous manner to those known for structure-bound hexokinase. (iv) With the binding of glycerol kinase to the mitochondria, it is possible to propose a metabolic pathway for glycerol oxidation to dihydroxyacetone phosphate by a combined action involving the enzyme, glycerol phosphate oxidase, and oxidative phosphorylation.

Adenosine Diphosphate↗
PubMed1982

Evolutionary changes in non-histone chromosomal proteins within the Drosophila melanogaster group revealed by monoclonal antibodies.

Monoclonal antibodies directed against nonhistone chromosomal proteins of D. melanogaster were tested for crossreactivity with the homologous antigens of various Drosophila species. -- By indirect immunofluorescence it could be shown that three antibodies react only with polytene chromosomes of species of the D. melanogaster subgroup, and only much less with chromosomes of other species of Drosophila. -- With chromosomes of various other species of the Sophophora or Drosophila radiations only a reaction at background level could be observed. The results suggest that the three antibodies react with different antigenic determinants of a single protein whose conformation changed rather fast during evolution of the Drosophilidae.

Animals↗
PubMed1982

[Shock lung].

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Adult↗