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Biomedical subjects

R Walter

Publications and source records attributed to R Walter.

At least 307 records · Page 17Linked to original sources
PubMed1970

Secondary structure of the cyclic moiety of the peptide hormone oxytocin and its deamino analog.

The secondary structure of the cyclic moiety of oxytocin and deamino-oxytocin has been determined by nuclear magnetic resonance spectroscopy (220 MHz). Oxytocin, in a dimethylsulfoxide-methanol mixture, contains a beta-turn involving the sequence -L-tyrosyl-L-isoleucyl-L-glutaminyl-L-asparaginyl-. Deamino-oxytocin, in addition to the beta-turn, contains a hydrogen bond involving the amide hydrogen of the tyrosine residue and the peptide carbonyl group of the asparagine residue, resulting in an antiparallel beta-type conformation for the ring component. An initial attempt has been made to relate conformational features of the hormonal peptides to their biological activity.

Chemical Phenomena↗
PubMed1970

Neurohypophyseal hormone-sensitive adenyl cyclase of toad urinary bladder.

An adenyl cyclase preparation derived from epithelial cells of the urinary bladder of the toad, Bufo marinus, is described. This cyclase preparation is specifically stimulated by neurohypophyseal hormones and various synthetic analogs which evoke a hydroosmotic response in the intact bladder. The relative stimulatory effects of these compounds have been compared on the cyclase preparation and in the intact bladder. The peptide concentrations required for half-maximal stimulation (affinity) in the cell-free and intact systems were parallel; however the magnitude of stimulation produced by saturating concentrations of peptides did not correlate. Furthermore, it was found that peptide analogs which inhibit the hydroosmotic effect of [8-arginine]-vasopressin on the intact bladder also inhibit the stimulation of the toad bladder cyclase preparation by vasopressin. Prostaglandin E(1), mercaptans, and disulfides, which inhibit the hormone-induced hydroosmotic response of the intact bladder, did not antagonize the stimulation of the toad bladder cyclase preparation by vasopressin.

Adenylyl Cyclases↗
PubMed1970

Threshold and receptor reserve in the action of neurohypophyseal peptides. A study of synergists and antagonists of the hydroosmotic response of the toad urinary bladder.

The interrelationship of several physiological receptors which influence the hydroosmotic response of the toad urinary bladder was studied employing neurohypophyseal peptides, prostaglandin E(1), theophylline, and cyclic nucleotides. The binding property of agonists (pD(2)), synergists (pS(2)), competitive antagonists (pA(2)), and noncompetitive antagonists (pD(2)') was determined after a suitable methodology had been developed. A series of neurohypophyseal peptides was examined in detail for their catalytic activity. It was found that the replacement of the hydroxy radical of the tyrosine residue in oxytocin by a methoxy and then by an ethoxy radical led to a progressive decline in the catalytic activity of the hormone-corresponding to a change from agonist to partial agonist to competitive antagonist. [4-Leucine]-mesotocin behaved as a competitive antagonist of oxytocin. Prostaglandin E(1) (PGE(1)) was found to be a noncompetitive inhibitor of neurohypophyseal peptides and theophylline; whereas the maximal hydroosmotic response of the bladder to [2-O-methyltyrosine]-oxytocin and theophylline was greatly depressed by PGE(1), the response to saturating concentrations of oxytocin was only slightly diminished-a finding which reveals a "receptor reserve" for oxytocin. Saturating concentrations of [2-O-ethyltyrosine]-oxytocin, inactive per se, potentiate theophylline-disclosing a "threshold phenomenon" for the mediation of neurohypophyseal hormone action. It is concluded that neurohypophyseal peptides are capable of producing graded effects on adenyl cyclase both below and above the range of enzyme activity which evokes graded changes in membrane permeability.

Adenylyl Cyclases↗
PubMed1969

Oxytocin: crystal data of a seleno analog.

The sulfur atom in position 6 of deamino-oxytocin (1-beta-mercapto-propionic acid-oxytocin) was replaced by selenium. The crystals of the resulting deamino-6-seleno-oxytocin are similar to those of the "wet" form of deamino-oxytocin, but they are stable upon prolonged exposure to air.

Crystallization↗
PubMed1969

Enzymatic inactivation of peptide hormones possessing a C-terminal amide group.

A partially purified enzyme extracted from the bladder of the toad, Bufo marinus L., was found to cleave the glycine amide moiety from oxytocin, 8-lysine-vasopressin, 8-arginine-vasopressin, and other hormone analogs terminating in a primary carboxamide group; however, this enzyme does not attack hormone analogs terminating with a methylamide, dimethylamide, or carboxyl group. Preliminary experiments indicate that a functionally similar enzyme is also present in the mammalian kidney, the major target organ of neurohypophyseal antidiuretic hormones. This enzyme, besides inactivating oxytocin and 8-lysine-vasopressin, also cleaves the phenylalanine amide moiety from a tetrapeptide analog of gastrin, another hormone terminating in a primary carboxamide group. Attention is drawn to the possible general significance of "carboxamidopeptidases" for the termination of the action of peptide hormones in which the C-terminal amino acid residue bears a carboxamide group.

Amides↗
PubMed1969

Oxytocin and neurohypophyseal peptides: spectral assignment and conformational analysis by 220 MHz nuclear magnetic resonance.

Magnetic resonance peaks have been assigned to individual protons of the constituent amino acids in the neurohypophyseal hormone, oxytocin, and in related peptides. The assignments were made possible by operation at 220 MHz with the use of variable temperature studies, proton homonuclear spin-decoupling, and comparison of spectra of oxytocin analogs. Some of the observed chemical shifts, and NH-CH(alpha) coupling constants were studied in relation to the conformation of the hormone.

Chemical Phenomena↗