Precise analysis of primary amino acids in urine by an automated high-performance liquid chromatography method: comparison with ion-exchange chromatography

2000 ◽  
Vol 744 (1) ◽  
pp. 183-188 ◽  
Author(s):  
Durk Fekkes ◽  
Ans Voskuilen-Kooyman ◽  
Robin Jankie ◽  
Jan Huijmans
Keyword(s):  
Amino Acids ◽  
High Performance Liquid Chromatography ◽  
High Performance ◽  
Method Comparison ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Chromatography Method ◽  
Precise Analysis ◽  
Primary Amino ◽  
Liquid Chromatography Method

Partial Primary Structure Of Human α2-Antiplasmin

1981 ◽  
Author(s):  
H R Lijnen ◽  
B Wiman ◽  
B Van Hoef ◽  
D Collen
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
High Performance Liquid Chromatography ◽  
High Performance ◽  
Gel Filtration ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Edman Degradation ◽  
Single Chain ◽  
Tryptic Digest

α2-Antiplasmin (α2AP), the main physiological inhibitor of plasmin in human plasma, is a single–chain glycoprotein with a molecular weight of 67,000 consisting of about 510 amino acids and containing 13 percent carbohydrate.A tryptic digest on 400 mg of reduced, carboxymethylated and citraconylated purified α2AP was performed. Peptides were separated by combinations of ion exchange chromatography, gel filtration and high performance liquid chromatography, and sequenced using the manual Edman degradation. Some peptides were further digested in order to establish overlaps. At the time of submission of this abstract we have sequenced 7 out of the approximately 21 arginyl peptides completely (each between 3 and 21 residues) and are working on the others. At present we have about 200 residues of sequence. Here we only report the stretches of 10 amino acids or more, which may be useful to compare the structure of α2AP with that of other serine protease inhibitors.

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