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Solid phase synthesis of ovine corticotropin releasing factor.

Ovine corticotropin releasing factor was synthesized by the stepwise solid phase method under conditions anticipated to maximize yield. Final yields of fully active hormone were 34% based on peptide which could be removed from the resin and 24% on initial resin substitution.

Amino Acid Sequence↗

Characterization of cleavage products in selected human lutropin preparations. A protease-sensitive site in human lutropin beta subunit.

Low molecular weight fragments derived from the beta subunit of human lutropin have been frequently observed. These fragments are detected by polyacrylamide gel electrophoresis in sodium dodecyl sulfate following reduction of the disulfide bonds. A sample of human lutropin was identified that had a major portion of its beta subunit showing this proteolytic nick. Over 83% of the subunit was nicked based on reduction, carboxymethylation, and isolation of the low molecular weight fragments. This preparation had 53% of the activity of an intact human lutropin (radioligand assay). The proteolytic nick in the subunit was shown by N-terminal sequencing of the C-terminal fragments to be derived from three clips in a hexapeptide region (residues 44-49) characterized by hydrophobic alkyl side chains. Specific clips were on the amino side of Leu-45 (8%), Val-48 (45%) and Leu-49 (47%). Thus the proteolytic activity, presumably derived from the pituitary during processing, has a substrate specificity reminiscent of the bacterial protease, thermolysin.

Alkylation↗

Identification of prostaglandins in prevertebral venous blood after preganglionic stimulation of the cat superior cervical ganglion.

1. In four out of seven experiments, prostaglandin-like activity was detected in prevertebral venous blood from the superior cervical ganglion, collected during and after preganglionic nerve stimulation.2. Prostaglandins E(1), E(2), F(2alpha) and a prostaglandin A were identified using solvent partition, column and thin-layer chromatography and bioassay techniques.3. The release of PGF(2alpha) was confirmed by combined gas chromatography-mass spectrometry.

Animals↗

Surface properties of Staphylococcus saprophyticus and Staphylococcus epidermidis as studied by adherence tests and two-polymer, aqueous phase systems.

S. saprophyticus is an established pathogen in man, devoided of characteristics associated with pathogenicity in Staphylococcus aureus. The ability of this species to attach to cells from regions, viz. the urinary tract, where it acts as an invador and to cells from areas where it is known as a commensal, was compared to its behaviour in this respect with another staphylococcal species, viz. S. epidermidis. S. saprophyticus showed a preferenital adherence to human exfoliated urogenital cells, when compared with its ability to attach to skin and buccal cells from man and also when compared with procine cells from these regions. The profound ability to adhere to human exfoliated urogenital epithelial cells by far exceeded that of S. epidermidis, while no such species difference was found when testing porcine cells (S. saprophyticus is unknown as a urogenital tract pathogen in pigs). When studied in a two-polymer, aqueous phase system, S. saprophyticus and S. epidermidis were found to have a negative surface charge at pH 7.2, but the former carried a considerably higher surface charge density. Both staphylococcal species exhibited a poor hydrophobic interaction liability. These physico-chemical surface characteristics are briefly discussed with regard to the differential bacteria-cell interactions of these species.

Adhesiveness↗

Countercurrent exchange of progesterone and antipyrine between human utero-ovarian vessels, and of antipyrine between the femoral vessels in the cat.

The utero-ovarian vein and ovarian artery in surgical specimens were cannulated and perfused in a countercurrent manner with isotonic, buffered solutions, fortified on the venous side with progesterone or radiolabelled methylantipyrine. Both substances were gradually transferred from the vein into the artery in the majority of the experiments while albumin was not exchanged. The results point to the existence of a countercurrent exchange mechanism in the human ovarian pedicle. Hardly detectable amounts of methylantipyrine were transferred from femoral vein to artery in the cat.

Animals↗