I would guess that you've not encountered lysosome-folk: they are masters of the centrifuge & all the protein isolation arts. de Duve was their Miyagi.
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I've actually worked on lysosomes (both in the cell as well as isolated), and have done more than my share of various subcellular fractionations. So my interest is in how you actually got the proteins themselves for analysis, not the organelle.
It is from the observations in GPMDB, although most of the data is not from lysosome-specific experiments. For example, there are 7,220 LC/MS/MS runs with data from SMPD1, corresponding to ~19,100 PSMs obtained from tissue & cell line preps.
Thanks Ron. What I am concerned about is when one doesn't know exactly how the different prep's/isolations/etc were done, we can't even begin to suspect if/how any PTM might have been lost in process.
Best think of it as a hypothesis (proving an absence is tough): based on ~600,000 proteomics experiments, there is no evidence that the enzymes in the lysosomal lumen have detectable S/T/Y phosphorylation, K acetylation/succinylation/sumoylation, R methylation/deimidation or S/T glycosylation.
Cheers.
As you say, proving the absence is tough and I don't think anyone probably wants to search through all those studies to assess the quality of protein recovery/isolation nor the analytical processes employed.
Databases and atlases are what they are.
Hope all is well out your way.
Comments
As you say, proving the absence is tough and I don't think anyone probably wants to search through all those studies to assess the quality of protein recovery/isolation nor the analytical processes employed.
Databases and atlases are what they are.
Hope all is well out your way.