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Biomedical subjects

E Glaser

Publications and source records attributed to E Glaser.

At least 73 records · Page 4Linked to original sources
PubMed1985

[Not Available].

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History, Modern 1601-↗
PubMed1984

[The course of pain in patients with confirmed duodenal ulcer under therapy with cimetidine].

In an open multicenter trial 1047 patients with endoscopically or X-ray verified duodenal ulcer were treated with 400 mg Cimetidin (Tagamet) b.i.d. The analysis of subjective pain records demonstrates 69% of the patients to suffer from severe pain before start of treatment while 3% were pain-free. Two days after start of treatment a statistically significant reduction (p less than 0.01) of intensity of pain has been proven. Five days after onset of treatment 30% of the patients are pain-free, 33% show minor impairment of well-being, 25% report moderate pain and 12% show clinically relevant pain.

Adult↗
PubMed1983

Kinetics of interaction between the H+-translocating component of the mitochondrial ATPase complex and oligomycin or dicyclohexylcarbodiimide.

Kinetics of interaction between the H+-translocating component of the mitochondrial ATPase complex and oligomycin or dicyclohexylcarbodiimide were studied in beef heart submitochondrial particles, and the results suggest that the two inhibitors have different binding sites with respect to the membrane and to F1. Oligomycin seems to be bound to a subunit or a part of a subunit in F0, which is localized superficially, and which is influenced by F1, since the presence of F1 considerably lowers the rate of inhibition. The oligomycin binding site further seems to be influenced by the different conformational states of F1 occurring during the catalytic cycle of the enzyme. The binding site of DCCD on F0, on the other hand, seems to be deeply embedded in the membrane and not influenced by F1.

Adenosine Triphosphatases↗
PubMed1983

[Ubiquitous and rare blood group related antigens and their significance in serology].

The present classification of some factors which are counted among the ubiquitary private and familiar as well as the rare and rarest antigens is shown. The classification of these antigens is often difficult. The distinguishing and systematisation of rare and rarest antigens requires of the investigator much consistency, responsibility and consideration as well as universal calmness so as not to bring too much confusion into an already broad palete of private and familiar antigens. Some antigens are frequently rearranged into already existing systems or even become independent. The authors boldly point out the variants of the ABO and Rh systems in which we meet with some ever so rare antigens, but which, as we know, are nevertheless not counted among the rare, in the sense of present comprehension. The practical value is pointed out and the need of improving our knowledge of ubiquitary, rare, familiar and private antigens in order to be able to master certain complications which these antigens would provoke in serology. In difficulties it is necessary to consult an experienced specialist in a well organised laboratory which possesses several different and reliable serums, the erythrocyte tests and a lot of experience.

Blood Group Antigens↗
PubMed1981

A study of the dicyclohexylcarbodiimide-binding component of the mitochondrial ATPase complex from beef heart.

1. The binding of [14C]-dicyclohexylcarbodiimide to membrane proteins of beef heart mitochondria has been investigated using dodecylsulphate/polyacrylamide gel electrophoresis. Upon incubation of submitochondrial particles with low concentrations of dicyclohexylcarbodiimide (5 nmol/mg protein) radioactivity was incorporated into three components with apparent molecular weights of 30000, 18000 and less than 6500. Only the two smaller components were found to be extracted into chloroform/methanol. The same two components were labelled when the isolated ATPase complex or a reconstituted F0F1 system was incubated with low concentrations of dicyclohexylcarbodiimide. High concentrations of dicyclohexylcarbodiimide (20-100 nmol/mg protein) resulted in binding to several mitochondrial proteins. 2. The maximal amount of dicyclohexylcarbodiimide which can bind to submitochondrial particles, the isolated ATPase complex, and the reconstituted F0F1 system was found to exceed the amount required for maximal inhibition of the ATPase activity by several-fold. The distribution of the bound [14C]dicyclohexylcarbodiimide between the different dicyclohexylcarbodiimide-binding components was investigated as a function of dicyclohexylcarbodiimide concentration. The smallest and largest components revealed a high affinity for dicyclohexylcarbodiimide-binding which paralleled the inhibition of ATPase activity. The intermediate component had a markedly lower affinity for dicyclohexylcarbodiimide-binding. 3. The larger dicyclohexylcarbodiimide-binding component of the isolated ATPase complex can be converted into the smaller component by treatment of the ATPase complex with performic acid. Partial conversion can also be achieved by extraction of the band from the dodecylsulphate-polyacrylamide gel after electrophoresis, followed by re-electrophoresis. The observations suggest that the larger component may be an oligomer of the smaller one. 4. Using concentrations of oligomycin and dicyclohexylcarbodiimide which were equal to or greater than those required for maximal inhibition of the ATPase activity, oligomycin was found to diminish the binding of [14C]dicyclohexylcarbodiimide to both dicyclohexylcarbodiimide-binding components of the isolated ATPase complex.

Adenosine Triphosphatases↗
PubMed1980

Reconstitution of mitochondrial oligomycin and dicyclohexylcarbodiimide-sensitive ATPase.

1. Oligomycin and dicyclohexylcarbodiimide-sensitive ATPase was isolated from beef-heart mitochondria and treated with 3.5 M NaBr in order to remove F1. The residue, called F0, was found to consist of seven components. Five of these are stained by Coomassie blue after dodecylsulfate-polyacrylamide-gel electrophoresis. Two of them correspond to the oligomycin-sensitivity-conferring protein and coupling factor F6, with apparent molecular weights of 21,000 and 9,400, respectively. Three additional polypeptides of molecular weights 23,000, 10,500 and 8,600 were not identified with known proteins. Two components not stained with Coomassie blue were detected by autoradiography of the gels of F0 preincubated with [14C]dicyclohexylcarbodiimide. These two components probably represent monomeric and oligomeric forms of the dicyclohexylcarbodiimide-binding protein. 2. F0 induced an oligomycin and dicyclohexylcarbodiimide-sensitive enhancement of K+ + valinomycin-driven proton translocation across the membrane of artificial phospholipid vesicles. 3. The interaction of F0 with purified, soluble beef heart F1 was investigated. F0 was capable of binding F1 and conferring oligomycin and dicyclohexylcarbodiimide sensitivity and cold stability on its ATPase activity. Furthermore F0 was found to diminish the specific activity of F1-ATPase. A comparison of these effects at varying F0/F1 ratios shows that F0 binds F1 in both an oligomycin-sensitive and an oligomycin-insensitive manner, and that both types of binding involve a conferral of cold stability and a decrease in specific activity. High F0/F1 ratios favoured in oligomycin-sensitive type of binding, indicating that F1 binds preferentially to oligomycin-sensitivity-conferring sites. Treatment of ATPase complex with trypsin resulted in an F0 with a decreased proportion of oligomycin-sensitivity-conferring binding sites and a diminished ability to lower the specific activity an cold lability of F1. 4. Reconstitution of F0 treated with trypsin and F1, oligomycin-sensitivity-conferring protein and F6 showed that at a constant amount of F1 bound, both oligomycin-sensitivity-conferring protein and F6 increased the oligomycin sensitivity of ATPase activity. It was therefore concluded that both of these coupling factors are involved in the conferral of oligomycin sensitivity. 5. The effect of the order of addition of F1, oligomycin-sensitivity-conferring protein and F6 to F0 on the reconstitution of oligomycin-sensitive ATPase activity, and of F1 and oligomycin-sensitivity-conferring protein to submitochondrial particles on the reconstitution of respiratory control, was investigated. The highest values of oligomycin sensitivity and respiratory control were obtained when F1 was added as the first component, indicating that F1 plays a directing role in the organisation of the components.

Adenosine Triphosphatases↗
PubMed1979

[Delirium tremens].

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Alcohol Withdrawal Delirium↗
PubMed1976

[Serological and clinical aspects of mass transfusion].

Massive transfusion of cold blood causes hemodinamic disturbances because of its acidity, surplus of potassium and defiency of calcium. Negative influence also results from stronger viscosity of blood, from the change of the active substances of blood coagulation, change of the patient's coagulation system responding to the transfused blood, subclinical troubles in this system according to the degree of the shock, reduced ability of oxygen transport caused by viscous blood, poor microcirculation etcr. Arrythmia, bradycardia, fibrilation of heart ventricles, may occur. Vasoconstrictions, microembolism and other incidents may appear. The quality of preserved blood changes during the conservation is changed, potassium and ATP are the indicators for its quality. At massive transfusions blood has to be warmed, filtered through special filters, to the patient has to be given just the quality of blood he needs etcr. The transfusiologist can help the therapist with useful advices and informations for the patient's sake.

Adenosine Triphosphate↗
PubMed1975

[Role of Zeta potentials in the Rh hemagglutination].

The structures of IgG are described. Actual length of IgG is about 240 A, of IgA about 350 A, of IgM 420 A. AHG must be of perfect quality, with right quantities of gamma and beta globulines and with specifical anticomplement. To cause the agglutination, we have to reduce repulsive powers of erytrocites and the Zeta potential, which we can reach sometimes with centrifuging as with use of physiological solutions and albumins. Described is the mechanism of this bringing together, too. IgM reacts optimal at Zeta potential 17-18 mV, IgM at 4, 5--8, 5 mV. Mast usable for this is the albumine of 22%.

Antibody Formation↗