scholarly journals Study of Saiga Horn Using High-Performance Liquid Chromatography with Mass Spectrometry

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Kateřina Mikulíková ◽  
Oleg Romanov ◽  
Ivan Miksik ◽  
Adam Eckhardt ◽  
Statis Pataridis ◽  
...  
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Free Amino ◽  
High Performance ◽  
Collagen Type ◽  
Polyacrylamide Gel Electrophoresis ◽  
Collagen Type I ◽  
Type I ◽  
Type Ii ◽  
Basic Representation

The saiga horns have been investigated the using of modern analytic methods. High-performance liquid chromatography (HPLC) with mass-spectrometric (MS and MS/MS) detection and polyacrylamide gel electrophoresis (PAGE) were used. It could be concluded that basic proteins of the saiga horns are keratins and collagen. The basic representation protein in all samples is keratin type I microfibrillar (from sheep), keratin type II microfibrillar (from sheep), collagen type I (α1) (from bovine) and collagen type I (α2) (from bovine). Free amino acids we determined in all samples are nontreated by enzyme.

scholarly journals Separation of collagen cyanogen bromide-derived peptides by reversed-phase high-performance liquid chromatography

1980 ◽  
Vol 191 (1) ◽  
pp. 253-256 ◽  
Author(s):  
M van der Rest ◽  
H P J Bennett ◽  
S Solomon ◽  
F H Glorieux
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
High Performance ◽  
Reversed Phase ◽  
Low Molecular Weight ◽  
Type I ◽  
Type Ii ◽  
Linear Gradient ◽  
Cnbr Cleavage ◽  
A New Technique

A new technique for separation of the CNBr cleavage products of collagen is described. It involves the use of a 30 nm pore reversed-phase high-performance liquid chromatography column eluted with a linear gradient of acetonitrile/water containing 0.01 M-heptafluorobutyric acid. The separation of type I, type II and type III CNBr peptides is described. Resolution is particularly good for the low-molecular-weight peptides. The method is fast, quantitative and sensitive, and the complete volatility of the eluent facilitates the recovery of the separated peptides.

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