Ideal for quality control, the amino acid composition of protein and peptide samples from a range of source material is determined by chemical hydrolysis.
Samples types include recombinant proteins from cell culture and fermentation material, nutraceuticals and plant materials.
Request Form: Amino Acid Analysis
The sample is on PVDF membrane, is it ok?
No, the protein must be lyophilised.
The sample is in liquid solution – is it OK?
No, please freeze dry prior to shipping to ensure maximum stability.
What quantity of proteins is required?
Our HPLC detection limit is 500 pmole per injection. With sample handling limitations this means nmoles of the target peptide are required. For proteins we require 10-100x this amount.
What to avoid when preparing a sample for amino acid analysis?
Purity of the sample is critical. This essentially means that 100% protein purity is required to obtain an accurate result. A 10% protein contamination can corrupt your final result.
Contamination with proteins, amino acids, buffers and salts will interfere with the analysis. Buffers containing primary and secondary amines, such as Glycine, Tris, HEPES and glycerol must be removed. These materials may be removed by ethanol-precipitation, trichloroacetic acid precipitation, reverse-phase extraction, gel filtration, ion-exchange separation, or dialysis.
What are the main problems encountered?
Cysteine and tryptophan cannot be analysed by conventional acid hydrolysis. They are destroyed in the hydrolysis process and require special hydrolysis methods.
Please indicate if you require cysteine and tryptophan analysis.
Asparagine and glutamine are 100% converted to aspartic and glutamic acids during acid hydrolysis of proteins and cannot be measured independently in a protein sample.
We require details on:
Please refer to the FAQs brochure for further answers.