Study of the natural antihistamine-like substance in bile of mammals

1976 ◽  
Vol 54 (4) ◽  
pp. 297-300
Author(s):  
Guy Pelletier ◽  
P. Gauthier ◽  
G. Laflamme ◽  
P. Coan ◽  
M. Lepage
Keyword(s):  
Amino Acids ◽  
Guinea Pig ◽  
Bile Acids ◽  
Solvent System ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Guinea Pig Ileum ◽  
Antihistamine Activity ◽  
Ileum Contraction ◽  
Layer Chromatography

A natural antihistamine substance (NAS) present in bile has been investigated. It was found that the antihistamine activity was not due to proteins, lipids, pigments, or amino acids. On ion exchange chromatography and thin-layer chromatography, this activity was associated with bile acids. Many bile acids could, in varying degrees, inhibit the histamine induced guinea pig ileum contraction, desoxycholic acid being the most potent. However NAS activity could be separated from bile acids and their conjugates using a different solvent system. Furthermore, NAS showed a higher antihistamine activity than bile acids. This substance seems to be responsible for 15–20% of the activity of whole bile. The substance has not yet been identified.

Preparation and properties of three analogues of [5-leucine]enkephalin, substrates for enzyme conversion studies

1985 ◽  
Vol 50 (6) ◽  
pp. 1329-1334
Author(s):  
Jaroslav Vičar ◽  
Linda Servítová ◽  
Martin Flegel ◽  
Karel Hauzer ◽  
Tomislav Barth
Keyword(s):  
High Pressure ◽  
Liquid Chromatography ◽  
Guinea Pig ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Guinea Pig Ileum ◽  
Opioid Activity ◽  
C Terminus ◽  
N Terminus ◽  
Fragment Condensation

Analogues of [5-Leu]enkephalin, prolonged by methionine on the N-terminus or, by lysine or methionine on the C-terminus were prepared by fragment condensation, purified by ion exchange chromatography or high-pressure liquid chromatography. The substances were characterised by their opioid activity in a test on guinea-pig ileum in comparison with the activity of [5-Leu]enkephalin.

Preparation and properties of a new dalargine analogue L-Tyr-D-Ala-Gly-L-Phe-L-Tle-L-Arg

1987 ◽  
Vol 52 (7) ◽  
pp. 1867-1871 ◽  
Author(s):  
Jan Pospíšek ◽  
Zhanna D. Bespalova ◽  
Eva Kovaříková ◽  
Michail I. Titov ◽  
Tomislav Barth ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Guinea Pig ◽  
Trifluoroacetic Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Guinea Pig Ileum ◽  
Stepwise Synthesis ◽  
Biologic Activity

Stepwise synthesis in solution provided tert-butyloxycarbonyl-O-benzyl-L-tyrosyl-D-alanyl-glycyl-L-phenylalanyl-L-tert-leucyl-L-arginine which was then catalytically reduced and treated with trifluoroacetic acid. The product was purified by ion exchange chromatography and free electrophoresis. The hexapeptide containing L-tert-leucine in position 5 exhibited 63% biologic activity (guinea pig ileum) of Dalargine (L-Tyr-D-Ala-Gly-L-Phe-L-Leu-L-Arg).

Post-proline endopeptidase, further characterization of the enzyme from pig kidneys

1984 ◽  
Vol 49 (8) ◽  
pp. 1846-1853 ◽  
Author(s):  
Karel Hauzer ◽  
Tomislav Barth ◽  
Linda Servítová ◽  
Karel Jošt
Keyword(s):  
Amino Acids ◽  
Aspartic Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Relative Molecular Mass ◽  
Enzyme Molecule ◽  
Thiol Compounds ◽  
Modified Method ◽  
N Terminus

A post-proline endopeptidase (EC 3.4.21.26) was isolated from pig kidneys using a modified method described earlier. The enzyme was further purified by ion exchange chromatography on DEAE-Sephacel. The final product contained about 95% of post-proline endopeptidase. The enzyme molecule consisted of one peptide chain with a relative molecular mass of 65 600 to 70 000, containing a large proportion of acidic and alifatic amino acids (glutamic acid, aspartic acid and leucine) and the N-terminus was formed by aspartic acid or asparagine. In order to prevent losses of enzyme activity, thiol compounds has to be added.

scholarly journals Free amino acids in fruit bodies of some wood destroying fungi

2014 ◽  
Vol 14 (1-2) ◽  
pp. 151-155
Author(s):  
Wiesław Tadeusiak ◽  
Eliza Balicka
Keyword(s):  
Amino Acids ◽  
Ion Exchange ◽  
Free Amino Acids ◽  
Free Amino ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Polyporus Squamosus

Concentration of free amino acids in the following bracket fungi: <i>Climacodon septentrionalis</i> (Fr) P. Karst, <i>Hapalopilus croceus</i> (Pers. ex Fr.) Donk., <i>Laetiporusus sulphurens</i> (Bull. ex Fr.) Murill and <i>Polyporus squamosus</i> Huds ex Fr., were determined by ion-exchange chromatography.

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