We are working with this sequence Leu-Gly-Gly-Ala-Lys-Gln-Ala-Gly-Asp-Val. If we treat with plasmin, which two ions it will generate. Can Plasmin digest any amino acid next to isopeptide bond.
Plasmin is the enzyme that acts on fibrinogen; then I wonder why you are using this specific sequence. I do not see similarity with any sequence in fibrinogen.
If you have MassSpect facility around you may incubate peptide and plasmin and test all the products.
I wonder whether this paper may be of help
In my experience, when you mix a protease with a protein, you will often see a reaction. The so-called "biological specificity", even for well-understood enzymes, is essentially irrelevant in limited reactions such as what you devised. By way of example, in some previous work (link is below), we demonstrated that thrombin (known for it's biological specificity for converting fibrinogen into fibrin) can have potent and wide-spread protease activity upon many blood-borne proteins. The suggestion of looking with mass spec is appropriate --> you may be surprised at what you find. I would recommend adding a time series to that experiment: incubate enzyme and substrate, and also remove (and denature) samples at a series of timepoints. The progress of cleavage reactions may not be uniform, and time is a critical factor to control.
(see https://www.researchgate.net/publication/23681065_Thrombin_induces_broad_spectrum_proteolysis_in_human_serum_samples)
Article Thrombin induces broad spectrum proteolysis in human serum samples
A simple BLAST search of LGGAKNAGDV will give you ~90% homology to a number of fibrinogen gamma chains.
Plasmin can cleave the K-N bond.
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