Experientia.
Discontinued
Publisher:
Birkhäuser Verlag
Frequency: Monthly
Country: Switzerland
Language: English
Start Year:1945 - 1996
Identifiers
| ISSN: | 0014-4754 (Print) 0014-4754 (Linking) |
| NLM ID: | 0376547 |
| (DNLM): | E19200000(s) |
| (OCoLC): | 01327195 |
| Coden: | EXPEAM |
| Classification: | W1 EX223 |
Sr2+ can become incorporated into an agonist-sensitive, cytoplasmic Ca2+ store in a cell line derived from the equine sweat gland epithelium. We have explored the properties of a Ca(2+)-dependent cell-signalling pathway that becomes active when cultured equine sweat gland cells are stimulated with ATP. The ATP-regulated, Ca(2+)-influx pathway allowed Sr2+ to enter the cytoplasm but permitted only a minimal influx of Ba2+. Experiments in which cells were repeatedly stimulated with ATP suggested that Sr2+, but not Ba2+, could become incorporated into the agonist-sensitive, cytoplasmic Ca2+ store. Further evidence for this was provided by experiments using ionomycin, a Ca2+ ionophore which has no affinity for Sr2+.
Vitamins and other metabolites in various sera commonly used for cell culturing. Many cell culture media use different sera to enhance growth. We assayed vitamins and some related metabolites in different sera and identified the concentration of: thiamin, biotin, folates, riboflavin, pantothenates, nicotinates, vitamins B6, B12, A, E, C, and carotenes and some related metabolites: biopterins, free inositol, free and total choline, total carnitines in chicken, horse, rabbit, goat, pig, calf, newborn calf, fetal calf and human sera. Results indicate that vitamin and metabolite content of different sera vary. Such variations could produce fluctuant effects on cell culturings ...
The regulatory peptide system of the large bowel in equine grass sickness. In recent years, distinct changes in regulatory peptides have been found in a number of gastrointestinal diseases. Grass sickness is a fatal disease of horses for which the etiology has yet to be fully ascertained. In this study, the peptide-containing nerves and ganglionic and mucosal endocrine cells of the ileum, colon and rectum were investigated in horses with sub-acute or chronic grass sickness and compared with normal controls using immunocytochemistry, at both the light and electron microscopical levels, and radioimmunoassay. A substantial loss of both peptide-containing cells and nerve...
Insensitivity of the ferritin iron core to heat treatment. To test whether the reactivity of ferritin iron is affected by the heat treatment used in ferritin isolation, we prepared ferritin from the same horse spleen with or without heating. Both samples exhibited similar reactivity upon reduction or chelation of iron.
A rapid and simple method for the isolation of pure eosinophilic leukocytes from horse blood. An improved and short method is described for the isolation of intact eosinophilic leukocytes from horse blood with high yield (1--1.5 g/20 l). Viability and purity of the preparations were verified by light and electron microscopy and by the trypan blue exclusion test. Isolated eosinophils were 98--100% pure, intact and viable, and they could be shown to phagocytise immune-complexes.
Specific reaction of aloe extract with serum proteins of various animals. We found that aloe extract contains a lectin-like substance which reacts with serum proteins of various animals. Furthermore, in human serum 2 proteins, alpha2-macroglobulin and alpha1-antitrypsin, were shown to be reactive with aloe extract.
The effect of ferrimyoglobin on the oxidation of succinic acid by horse heart muscle preparations. In a series of model reactions, it is shown that residues
of ~-aminoacids may be inserted by a particular rearrangement into certain carboxyl or carbonylamido
groups. Repeated insertion results in the formation of
a peptide derivative. It is concluded that natural peptides or proteins must not necessarily be formed by head
to tail combination of aminoacids, Other implications of
the new principle are discussed.
[Changes of the serum cholinesterase in the horse as measured by paper electrophoresis]. The paper-electrophoresis of horse-serum has shown, that the cholinesterase migrates with the β-globulin-fraction.