Reversed phase high-performance liquid chromatography (RPHPLC) coupled with electrospray ionization mass spectrometry (ESI-MS) was used to separate and characterize the peptides resulting from the tryptic cleavage of somidobove, a recombinant bovine growth hormone. The tryptic digestion of somidobov
Separation of the tryptic peptides from reduced, alkylated hen egg white lysozyme by high-performance liquid chromatography
โ Scribed by L. Haeffner-Gormley; N.H. Poludniak; D.B. Wetlaufer
- Publisher
- Elsevier Science
- Year
- 1981
- Tongue
- English
- Weight
- 812 KB
- Volume
- 214
- Category
- Article
- ISSN
- 1873-3778
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โฆ Synopsis
We describe high-performance liquid chromatographic systems for the separation of the tryptic peptides of reduced, alkylated hen eggwhite lysozyme. The resolved peptides which contained 3-23 amino acid residues were identified by determinytion of amino acid composition.
Gradients of acetonitrile with aqueous ammonium acetate or ammonium chloride were employed to elute from a reversed-phase C,, column, monitoring absorbance at 205 nm. 2 12 nm or 280 nm. Peptides containing Scarboxymethyl-cysteine eluted more rapidly than the corresponding S-ethylsuccinimido peptides.
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