A: protein 1, protein 2 and protein 3, combined together, and then are totally hydrolyzed (ensure enough time)
B: Only protein 1 is hydrolyzed under same conditions like A (of course different E/S).
As for the peptide composition from protein 1, are there any differences?
When I read a research about determination of protein content by LC-MS with specific peptide standards I get puzzled.
So anyone have some idea about these? Thank you in advance.
For MS you require pure protein digested with proteases like trypsin - which would give you polypeptides of definite length which can be matched with database and further MS MS may be done.
If you use protein mixture - i suppose digestion would be ok - but on MS you would be confused on identity - it would not be of help
Dear Vivek,
There are many different samples, all of them are protein mixtures and include protein 1. Authors find a specific enzymatic peptide, only produced via protein 1, and they also find a linear response between content of pure protein 1 and content of this specific peptide.
So they test the contents of protein 1 in different samples with this synthetic specific peptide as an internal standard by LC-MS.
But, in different mixtures, is there no effect coursed via other proteins on this linear response?
When protein1 mixed with other proteins, for the enzymatic hydrolysis, the contents of this peptide released via protein1 will keep stable just like it in the pure form?
Of course, I think authors keep all the samples totally hydrolyzed.
- Badges
- Science topic
- Similar topics
- Biological Science
- Molecular Biology
- Biomolecules
- Proteins