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S Castensson

Publications and source records attributed to S Castensson.

16 recordsLinked to original sources
PubMed1982

Occurrence of an insulin-like peptide in extracts of peripheral nerves of th cat and in extracts of human vagal nerves.

Biopsies from various peripheral nerves were collected from living cats. The biopsies were extracted with acid ethanol and the insulin-like immunoreactivity (ILI) content of the extracts determined with radioimmunoassay. The vagal, sciatic and radial nerves contained on the average 90, 3 and 28 ng of ILI per gram nerve tissue (wet weight), respectively. In the sympathetic trunc no ILI was found. In order to partly purify and characterize the nerve ILI extracts these were run on an HPLC system. the ILI coeluted with standard bovine insulin. The same amounts of ILI were found in the nerve extracts whether run on the HPLC system or not. It can be concluded that all of the immunoreactive material of the nerve extracts corresponds to insulin or to a peptide very similar to insulin. In two cats the radial and sciatic nerves were ligated for 24 h. Two to ten times more ILI occurred in biopsies taken proximal to the site of ligation than in those from corresponding distal biopsies, indicating that the insulin-like material is transported distally within the nerves. ILI was found in extracts from vagal nerves taken from 3 days old human autopsy material. Also this human ILI coeluted with the bovine insulin standard in the HPLC system.

Animals↗
PubMed1979

Tripeptide analogues of melanocyte-stimulating hormone release-inhibiting hormone (Pro-Leu-Gly-NH2) as inhibitors of oxotremorine-induced tremor.

Fourteen di- and tripeptide analogues of MIF, Pro-Leu-Gly-NH2, have been synthesized and assayed for inhibition of oxotremorine-induced tremor. Replacement of Pro by HCO-Pro or cyclopentanecarboxylic acid gave inactive analogues, while some peptides of the general structure less than Glu-Leu-Gly-NR1R2 were highly active. Thus, R1 = C3H8 and R2 = H gave 4 times the activity of MIF, R1 = I-C3H8 and R2 = H gave 13 times the activity of MIF, and R1 = R2 = CH3 gave 29 times the activity of MIF. cyclo(-Pro-Leu-), Pro-Lys-Gly-NH2, and Pro-Arg-Gly-NH2 had no activity. Apparently, small modifications in the structure of MIF can yield highly active analogues with potential clinical value, e.g., in the treatment of Parkinson's disease or mental depression.

Animals↗
PubMed1979

Characterization of mutationally altered dihydropteroate synthase and its ability to form a sulfonamide-containing dihydrofolate analog.

Among spontaneous mutants of Escherichia coli selected for resistance against sulfonamides, thermosensitive strains were found. These were shown to possess a changed dihydropteroate synthase (EC 2.5.1.15), which had a substantially higher Km value for its normal substrate, p-aminobenzoic acid, and an about 150-fold higher Km for sulfonamides. The mutationally changed dihydropteroate synthase was found to be thermosensitive by in vitro assays. The thermosensitivity was used as an enzyme marker to demonstrate the complex formation between 2-amino-4-hydroxy-6-pyrophosphorylmethyl pteridine and sulfonamides by partially purified dihydropteroate synthase. The formation of folate from 2-amino-4-hydroxy-6-pyrophosphorylmethyl pteridine and p-aminobenzoylglutamic acid by dihydropteroate synthase was found to be very sensitive to inhibition by sulfonamides and very inefficient with the mutationally changed enzyme.

4-Aminobenzoic Acid↗