Analysis and purification of modified methoxy(polyethylene glycol) compounds of similar molecular mass by high-performance liquid chromatography

1995 ◽  
Vol 704 (2) ◽  
pp. 369-376 ◽  
Author(s):  
William H. Leister ◽  
Larry E. Weaner ◽  
Donald G. Walker
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Polyethylene Glycol ◽  
Molecular Mass ◽  
High Performance ◽  
Methoxy Polyethylene Glycol

Separation of high-molecular mass RNAs by high-performance liquid chromatography on hydroxyapatite

1990 ◽  
Vol 515 ◽  
pp. 611-619 ◽  
Author(s):  
Shinichiro Hori ◽  
Sachiko Ohtani ◽  
Kenji Miyazaka ◽  
Toshihiro Ishikawa ◽  
Hitoshi Tanabe
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Molecular Mass ◽  
High Performance ◽  
High Molecular Mass

Angiotensin I–Converting Enzyme Inhibitory Activity of Peptides Derived from Egg White Proteins by Enzymatic Hydrolysis

2004 ◽  
Vol 67 (9) ◽  
pp. 1914-1920 ◽  
Author(s):  
M. MIGUEL ◽  
I. RECIO ◽  
J. A. GÓMEZ-RUIZ ◽  
M. RAMOS ◽  
R. LÓPEZ-FANDIÑO
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Molecular Mass ◽  
Inhibitory Activity ◽  
High Performance ◽  
Egg White ◽  
Reversed Phase ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

The hydrolysis of crude egg white with pepsin, trypsin, and chymotrypsin produced peptides with angiotensin-converting enzyme (ACE) inhibitory properties. These peptides were mainly derived from the proteolysis of ovalbumin. The most active hydrolysates were obtained after treatment with pepsin (50% inhibitory concentration [IC50], 55.3 μg/ml), with the fraction having a molecular mass lower than 3,000 Da giving the highest ACE inhibitory activity (IC50, 34.5 μg/ml). Nine subfractions were collected from the fraction with a molecular mass lower than 3,000 Da using semipreparative reversed-phase high-performance liquid chromatography. Considerable ACE inhibitory activity (IC50 < 40 μg/ml) was found in three of them. These subfractions were analyzed by reversed-phase high-performance liquid chromatography–tandem mass spectrometry, and 14 peptides were identified. These sequences were synthesized, and their ACE inhibitory activities were measured. Among the identified peptides, two novel sequences with potent ACE inhibitory activity were found. The amino acid sequences of these inhibitors were identified as Arg-Ala-Asp-His-Pro-Phe-Leu and Tyr-Ala-Glu-Glu-Arg-Tyr-Pro-Ile-Leu and showed IC50 values of 6.2 and 4.7 μM, respectively.

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