Bleaching action of extract of the mucosa and submucosa of the human appendix on melanophores of the frog skin

1974 ◽  
Vol 78 (2) ◽  
pp. 955-957
Author(s):  
N. T. Raikhlin ◽  
I. M. Kvetnoi
Keyword(s):  
Frog Skin ◽  
Bleaching Action ◽  
Human Appendix

Analysis of Individual Frog Skin Extracts from Dendrobates Auratus with Capillary NMR

Planta Medica ◽  
2013 ◽  
Vol 79 (10) ◽  
Author(s):  
RW Fitch ◽  
A Weng ◽  
RA Saporito
Keyword(s):  
Frog Skin ◽  
Dendrobates Auratus

The Sigma-1 Receptor Ligands Chlorpromazine and Trifluoperazine Inhibit Na+ Transport in Frog Skin Epithelium

BIOPHYSICS ◽  
2020 ◽  
Vol 65 (5) ◽  
pp. 784-787
Author(s):  
A. V. Melnitskaya ◽  
Z. I. Krutetskaya ◽  
V. G. Antonov ◽  
N. I. Krutetskaya
Keyword(s):  
Frog Skin ◽  
Receptor Ligands ◽  
Na Transport ◽  
Sigma 1 Receptor ◽  
Skin Epithelium ◽  
Frog Skin Epithelium ◽  
Sigma 1

The melanocyte stimulating activity of N-nitroso-2-chloroethyl-carbamoyl derivatives of α-melanotropin fragments

1988 ◽  
Vol 53 (11) ◽  
pp. 2574-2582 ◽  
Author(s):  
Hedvig Medzihradszky-Schweiger ◽  
Helga Süli-Vargha ◽  
József Bódi ◽  
Kálmán Medzihradszky
Keyword(s):  
Biological Activity ◽  
Active Site ◽  
Frog Skin ◽  
Terminal Sequence ◽  
Subsequent Reaction ◽  
Affinity Labels ◽  
Derivatives Of

A number of N-nitroso-2-chloroethyl-carbamoyl (Q(NO)) derivatives of α-melanotropin fragments have been synthesized and their effect on the frog skin melanocytes studied. Peptides substituted in this way possess the biological activity of the parent compounds, indicating that they preserved their receptor recognizing ability. These compounds can therefore serve as affinity labels. Some of these derivatives, related to the C-terminal sequence of α-melanotropin show prolonged darkening reaction, which does not influence the subsequent reaction of melanocytes with α-melanotropin. The Q(NO)-derivative of a fragment derived from the classical active site of the hormone shows, however, inhibition of the effect of α-melanotropin. It can be concluded that the latter peptide acts through the melanotropin receptor, while others, related to the C-terminal sequence of the hormone through another mechanism.

Global Na+ diffusion coefficient in a multicompartment frog skin epidermis model

1977 ◽  
Vol 68 (1) ◽  
pp. 161-165 ◽  
Author(s):  
Ernst G. Huf ◽  
John R. Howell
Keyword(s):  
Diffusion Coefficient ◽  
Frog Skin ◽  
Skin Epidermis

Antimicrobial properties of the frog skin peptide, ranatuerin-1 and its [Lys-8]-substituted analog

Peptides ◽  
2004 ◽  
Vol 25 (1) ◽  
pp. 29-36 ◽  
Author(s):  
Agnes Sonnevend ◽  
Floyd C. Knoop ◽  
Mahrendra Patel ◽  
Tibor Pál ◽  
Ana Maria Soto ◽  
...  
Keyword(s):  
Frog Skin ◽  
Antimicrobial Properties

Seasonal changes of antidiuretic hormone action on sodium transport across frog skin

1968 ◽  
Vol 215 (2) ◽  
pp. 439-443 ◽  
Author(s):  
SK Hong ◽  
CS Park ◽  
YS Park ◽  
JK Kim
Keyword(s):  
Antidiuretic Hormone ◽  
Sodium Transport ◽  
Seasonal Changes ◽  
Frog Skin ◽  
Hormone Action

pHi determines rate of sodium transport in frog skin: results of a new method to determine pHi

1994 ◽  
Vol 266 (3) ◽  
pp. F367-F374 ◽  
Author(s):  
R. Rick
Keyword(s):  
Frog Skin ◽  
Nuclear Potential ◽  
Na Channel ◽  
Cytoplasmic Ph ◽  
Na Transport ◽  
Principal Cells ◽  
Weak Organic Acid ◽  
Transepithelial Na Transport ◽  
Cell Layers ◽  
Important Regulator

The pH of the isolated frog skin epithelium was determined on a cellular and subcellular level based on the distribution of a weak organic acid, 4-bromobenzoic acid. The indicator is detectable by X-ray microanalysis due to the presence of an element label. The results show that the pH of principal cells, but not the Na concentration, is closely correlated with the rate of transepithelial Na transport. Acidification leads to an inhibition of Na transport, regardless of whether the change was spontaneous or experimentally induced. Under the conditions of this study, the pH of principal cells was not well regulated. At a bath pH of 7.0, large pH differences between the cell layers were detectable. In mitochondria-rich cells, the pH was a function of the intracellular Cl concentration but not the Na transport rate. The cytoplasmic pH consistently exceeded the nuclear pH. The nuclear-cytoplasmic pH differential in principal cells amounted to 0.3 pH units, which is equivalent to a nuclear potential of -17 mV. The results support the view that the intracellular pH (pHi) is an important regulator of transepithelial Na transport. Regulation is primarily achieved at the level of the apical Na channel, making the Na influx the rate-limiting step in Na reabsorption.

The effect of T-2 toxin on active sodium transport across frog skin in the presence of ADH and amphotericin B

1989 ◽  
Vol 93 (1) ◽  
pp. 33-36 ◽  
Author(s):  
E. Gallucci ◽  
L. Barbarossa ◽  
A. Bottalico ◽  
D. Angiolillo ◽  
S. Micelli
Keyword(s):  
Amphotericin B ◽  
Sodium Transport ◽  
Frog Skin ◽  
Active Sodium ◽  
Active Sodium Transport

Ultrasonic production of reversible changes in the electrical parameters of isolated frog skin

1976 ◽  
Vol 60 (1) ◽  
pp. 225-229 ◽  
Author(s):  
A. J. Coble ◽  
F. Dunn
Keyword(s):  
Frog Skin ◽  
Electrical Parameters
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