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Biomedical subjects

V J Hruby

Publications and source records attributed to V J Hruby.

At least 487 records · Page 27Linked to original sources
PubMed1972

Melanophore stimulating hormone: release inhibition by ring structures of neurohypophysial hormones.

Tocinamide and tocinoic acid, ring structures of oxytocin, are potent inhibitors of the release of melanophore stimulating hormone from the rat and hamster pituitary in vitro. Tocinamide is effective at concentrations as low as 10-(14)M on the mammalian pituitary. These peptides do not affect release of the hormone on the frog (Rana pipiens) pars intermedia, but they do inhibit release in the bullfrog (Rana catesbeiana) and the toad (Bufo marinus). The specificity of the peptides on inhibition of the hormone is demonstrated by the fact that oxytocin, lysine vasopressin, and pressinoic acid and pressinamide (ring structures of the vasopressins) do not show such inhibitory activity. Hypothalamic extracts of either the frog (Rana pipiens) or the rat inhibit release of the hormone from pituitaries of either species. The inhibitory effects of tocinamide and tocinoic acid, like that of hypothalamic extracts, are reversible.

Animals↗
PubMed1972

Conformational studies on tocinamide and deaminotocinamide by 220 MHz nuclear magnetic resonance spectroscopy.

The 220 MHz spectra of tocinamide and deaminotocinamide, the ring moieties of oxytocin and of deamino-oxytocin, respectively, were investigated in [U-(2)H]dimethylsulfoxide solution. Extensive decoupling and exchange experiments allow complete spectral assignment and determination of many coupling constants. Circular dichroism spectra assigned a right-hand screw sense to the C-S-S-C group. The conformations of tocinamide and deaminotocinamide are different from each other and from those suggested for the ring portions of oxytocin and deamino-oxytocin. The relationship of this difference to biological activity is commented upon. The importance of the interaction of the side chain with the ring in oxytocin and deamino-oxytocin is emphasized.

Chemical Phenomena↗
PubMed1971

NMR studies on the conformation of derivatives of the side chain of oxytocin: examples of cis-trans isomerism.

The 220 MHz spectra reported in this paper show the existence of cis-trans isomerism about the Cys-Pro bond in (S-benzyl)-L-Cys-L-Pro-L-Leu-Gly(NH(2)) and about the Z-Pro bond in (N-benzyloxycarbonyl)-L-Pro-L-Leu-Gly(NH(2)). These peptides are derivatives of the side chain of oxytocin, which has the structure L-Pro-L-Leu-Gly(NH(2)). Taken in water-free (CD(3))(2)SO, the spectra also show differences between the two isomers in the amide chemical shifts, which indicate interaction of the terminal end of the peptides with the rest of the residues. The ratio of the isomeric forms is about 2:3 for the S-benzylcysteinyl peptide, while it is 1:1 for the N-benzyloxycarbonyl-protected peptide. The probable assignment of peaks in isomers is discussed, in addition to routine spectral assignments based on extensive decoupling experiments.

Amino Acid Sequence↗
PubMed1969

Deuterated oxytocins: the synthesis and biological properties of a crystalline analog of deamino-oxytocin deuterated in the 5-asparagine position.

This paper describes the synthesis and biological activity of [5-L-asparagine-alpha,beta,beta-d(3)]-deamino-oxytocin. The model peptide S-benzyl-beta-mercaptopropionyl-L- asparaginyl-alpha,beta,beta-d(3)-glycinamide was also prepared to observe the effect of the conditions of peptide synthesis on the deuterium content. It was found that normal synthetic procedures could be used without a significant loss in the deuterium content.The [5-L-asparagine-alpha,beta,beta-d(3)]-deamino-oxytocin had, within experimental error, the same avian vasodepressor and oxytocic activities as deamino-oxytocin itself.

Amino Acid Sequence↗
PubMed1968

4-Leucine-oxytocin: natriuretic, diuretic, and antivasopressin polypeptide.

During water diuresis in anesthetized rats, 4-leucine-oxytocin increased the urine output and the rates of sodium and chloride excretion. The potassium excretion rate was only slightly increased. During vasopressin-suppressed water diuresis, 4-leucine-oxytocin produced similar effects on urine and electrolyte excretions. In addition, it inhibited the vasopressin-induced free-water reabsorption, and it could reverse reabsorption to freewater clearance.

Absorption↗
PubMedDate not supplied

Structural characteristics of two highly selective opioid peptides.

The demonstration of opioid receptors by radioligand binding and the discovery of their endogenous peptide ligands has provided a new class of compounds that can be used for the development of novel opioids. The number of potential receptor targets for such opioids has been expanded by the identification of multiple opioid receptor types. The development of highly selective opioid peptides using the principles of conformational restriction permits the analysis of the structure-activity requirements of each receptor type, and is facilitating the elucidation of the functional properties of the different opioid receptors.

Animals↗