Amino acids and peptides. LXXI. Synthesis of 1-deamino-8-D-γ-aminobutyrine-vasopressin, 1-deamino-8-D-lysine-vasopressin, and 1-deamino-8-D-arginine-vasopressin

1967 ◽  
Vol 32 (3) ◽  
pp. 1250-1257 ◽  
Author(s):  
M. Zaoral ◽  
J Kolc ◽  
F. Šorm
Keyword(s):  
Amino Acids ◽  
Arginine Vasopressin ◽  
Lysine Vasopressin

EFFECTS OF ARGININE-, LYSINE- AND LEUCINE-VASOPRESSIN ON URINARY OSMOLALITY AND RATE OF URINE FLOW IN HYDRATED RATS AND DOGS

1959 ◽  
Vol XXXII (I) ◽  
pp. 134-141 ◽  
Author(s):  
Niels A. Thorn
Keyword(s):  
Arginine Vasopressin ◽  
Urine Osmolality ◽  
Urine Flow ◽  
The Other ◽  
Maximum Increase ◽  
Urinary Osmolality ◽  
Lysine Vasopressin

ABSTRACT Arginine-, lysine- and leucine-vasopressin, injected i. v. into hydrated rats or dogs caused different patterns of response in that urine osmolality fell much more slowly after the maximum increase following arginine-vasopressin, than after the other two preparations. Using 3 different parameters for antidiuretic response, arginine-vasopressin was somewhat more potent than leucine-vasopressin in both rats and dogs, considerably more potent than lysine-vasopressin in rats, and much more so in dogs.

Amino acids and peptides. LI. Synthesis of 2-O-methyltyrosine- and 2-O-ethyltyrosine-lysine-vasopressin

1965 ◽  
Vol 30 (6) ◽  
pp. 1869-1873 ◽  
Author(s):  
M. Zaoral ◽  
E. Kasafírek ◽  
J. Rudinger ◽  
F. Šorm
Keyword(s):  
Amino Acids ◽  
Lysine Vasopressin

Binding and internalization of a fluorescent vasopressin analogue by collecting duct cells

1988 ◽  
Vol 255 (5) ◽  
pp. C622-C632 ◽  
Author(s):  
K. L. Kirk
Keyword(s):  
Arginine Vasopressin ◽  
Collecting Duct ◽  
Computer Assisted ◽  
Principal Cells ◽  
Lysine Vasopressin ◽  
Collecting Tubule ◽  
Basal Pole ◽  
V2 Receptor ◽  
Tubule Cells ◽  
Maximal Binding

The kinetics of binding and internalization of a fluorescent vasopressin analogue [1-desamino-8-rhodamine lysine vasopressin (rhoda LVP)] by principal cells within the microperfused rabbit cortical collecting tubule were quantitatively assessed with computer-assisted video microscopy. At 25 degrees C, binding of rhoda LVP exhibited saturation kinetics with half-maximal binding at 2 nM and maximal binding at concentrations greater than 5 nM. Rhoda LVP binding could be prevented by the simultaneous addition of a 10-fold higher concentration of arginine vasopressin (AVP) or the V2-receptor agonist, 1-desamino-8-D-arginine vasopressin (desmopressin). No obvious internalization or rhoda LVP was detected at 25 degrees C, i.e., the rhoda LVP fluorescence remained localized to the basal pole of each principal cell for at least 100 min after rhoda LVP addition and could be largely reversed by the subsequent addition of AVP. Conversely, warming the cells to 38 degrees C after binding was initiated resulted in a rapid (less than 30 min) migration of the fluorescence into the cell interior and a loss of AVP-displaceable binding from the cell surface. These results document the utility of this noninvasive optical strategy for quantitatively monitoring hormone binding to intact collecting tubule cells and demonstrate that rhoda LVP binds reversibly and with high affinity to V2 receptors on principal cells in the collecting tubule. The internalization (and presumed inactivation) of the hormone-receptor complex at 38 degrees C may contribute to the desensitization of collecting tubule cells to vasopressin at physiological temperature.

A specific antibody to vasopressin in a man with concomitant resistance to treatment with Pitressin.

1986 ◽  
Vol 32 (1) ◽  
pp. 211-212 ◽  
Author(s):  
D G Bichet ◽  
C Kortas ◽  
C Manzini ◽  
J N Barjon
Keyword(s):  
Diabetes Insipidus ◽  
Arginine Vasopressin ◽  
Specific Antibody ◽  
Specific Binding ◽  
Cross Reactivity ◽  
Resistance To Treatment ◽  
Allergic Symptoms ◽  
Lysine Vasopressin ◽  
Concomitant Resistance ◽  
Neurogenic Diabetes Insipidus

Abstract A 26-year-old man with complete neurogenic diabetes insipidus since age nine was initially treated with vasopressin (Pitressin Tannate in oil). At age 13, its dosages were progressively increased to control the patient's polyuria; minor allergic symptoms occurred after every such treatment. We incubated serial dilutions of the patient's plasma with 125I-labeled arginine-vasopressin and obtained a 50% specific binding for the plasma at a final dilution of 625-fold. Cross-reactivity studies showed that lysine-vasopressin was better recognized by the antibody than arginine-vasopressin. These results were attributed to large concentrations of lysine-vasopressin (pork vasopressin) in the Pitressin.

4-Phenylalanine analogues of vasopressin: Synthesis, pharmacological and chiroptical properties

1986 ◽  
Vol 51 (7) ◽  
pp. 1532-1541 ◽  
Author(s):  
František Brtník ◽  
Tomislav Barth ◽  
Petr Maloň ◽  
Ivo Frič ◽  
Vija E. Kluša ◽  
...  
Keyword(s):  
Arginine Vasopressin ◽  
Pharmacological Properties ◽  
Cd Spectra ◽  
Chiroptical Properties ◽  
Lysine Vasopressin ◽  
Vasopressin Synthesis

Synthesis, some pharmacological properties and CD spectra of [4-phenylalanine, 8-arginine]vasopressin and [4-phenylalanine, 8-lysine]vasopressin are described.

THE DEVELOPMENT OF A RADIOIMMUNOASSAY FOR OXYTOCIN: SENSITIVITY OF THE ASSAY IN AQUEOUS BUFFER SOLUTION, SPECIFICITY AND THE DISSOCIATION OF IMMUNOLOGICAL AND BIOLOGICAL ACTIVITY

1970 ◽  
Vol 46 (4) ◽  
pp. 533-542 ◽  
Author(s):  
T. CHARD ◽  
M. L. FORSLING ◽  
M. A. R. JAMES ◽  
M. J. KITAU ◽  
J. LANDON
Keyword(s):  
Aqueous Solution ◽  
Biological Activity ◽  
Arginine Vasopressin ◽  
Late Pregnancy ◽  
Reducing Agents ◽  
Immunological Activity ◽  
Buffer Solution ◽  
Aqueous Buffer ◽  
Lysine Vasopressin ◽  
Other Substances

SUMMARY A radioimmunoassay for oxytocin in aqueous solution is described, with a sensitivity comparable with the best current bioassays. It is highly specific; arginine-vasopressin and lysine-vasopressin interfere only at 1000-fold greater concentration, while bradykinin, histamine, acetycholine and many other substances, which interfere with some bioassays, have no effect. In certain circumstances, there is a dissociation between loss of biological and immunological activity. Thus reducing agents had no effect on immunological activity, in contrast to their effect on biological activity. In late pregnancy plasma, the biological activity of oxytocin is destroyed more rapidly than the immunological activity. Radioimmunoassays have considerable advantages over bioassays both in convenience and specificity. However, bioassays should be employed for reference purposes because of the dissociation between biological and immunological activity that may occur.

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