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).

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.

Purification of IgG from Sera of Rabbit and Guinea Pig by Flow-Through Mode Ion-Exchange Chromatography using DEAE Sepharose Fast Flow Column

2011 ◽  
Vol 74 (3-4) ◽  
pp. 209-214 ◽  
Author(s):  
Ying Wang ◽  
Peiyin Zhang ◽  
Shujun Liu ◽  
Yongsheng Zhang ◽  
Tiesuo Zhao ◽  
...  
Keyword(s):  
Ion Exchange ◽  
Guinea Pig ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Flow Through ◽  
Fast Flow

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.

Studies on an Inhibitor of Plasminogen Activation in Human Serum

1973 ◽  
Vol 30 (02) ◽  
pp. 414-424 ◽  
Author(s):  
Ulla Hedner
Keyword(s):  
Ion Exchange ◽  
Human Serum ◽  
Antithrombin Iii ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Specific Adsorption ◽  
Partial Purification ◽  
Plasminogen Activation ◽  
Preparative Electrophoresis

SummaryA procedure is described for partial purification of an inhibitor of the activation of plasminogen by urokinase and streptokinase. The method involves specific adsorption of contammants, ion-exchange chromatography on DEAE-Sephadex, gel filtration on Sephadex G-200 and preparative electrophoresis. The inhibitor fraction contained no antiplasmin, no plasminogen, no α1-antitrypsin, no antithrombin-III and was shown not to be α2 M or inter-α-inhibitor. It contained traces of prothrombin and cerulo-plasmin. An antiserum against the inhibitor fraction capable of neutralising the inhibitor in serum was raised in rabbits.

Review on the Application of Mixed-mode Chromatography for Separation of Structure Isoforms

2018 ◽  
Vol 20 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Tsutomu Arakawa
Keyword(s):  
Ion Exchange ◽  
Mixed Mode ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Charged State ◽  
Partial Structure ◽  
Reverse Phase ◽  
Oligomer Formation ◽  
Structure Rearrangement ◽  
Disulfide Scrambling

Proteins often generate structure isoforms naturally or artificially due to, for example, different glycosylation, disulfide scrambling, partial structure rearrangement, oligomer formation or chemical modification. The isoform formations are normally accompanied by alterations in charged state or hydrophobicity. Thus, isoforms can be fractionated by reverse-phase, hydrophobic interaction or ion exchange chromatography. We have applied mixed-mode chromatography for fractionation of isoforms for several model proteins and observed that cation exchange Capto MMC and anion exchange Capto adhere columns are effective in separating conformational isoforms and self-associated oligomers.

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