Here again is the brief from my professor as a reply to the doc's claims -
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he purity of the protein is determined by SDS-PAGE in presence of reducing agent which shows the purity and the approximate molecular mass of the protein. However as SDS-PAGE is conducted in presence of detergent (SDS) it does not distinguish between non-covalent oligomers or dimers. Therefore we also test the protein by size exclusion chromatography (SEC) in buffer pH 8 without detergent which is capable to show whether the tested protein is a pure monomer. Once both tests are positive no additional test by Mass Spectrometry (MS) is required. However MS tests were occasionally performed and when tested they always showed over 95-98% purity and the expected molecular mass of about 22106 or 22130 Da. Please note that in some cases the stained molecular mass standards are not accurate. Thus for example molecular mass standards showed inaccurate molecular mass of hGH of ~19 kDa, while mass spectrometry of the same sample (in two tests) showed molecular mass of 22,106 and 22,130 Dalton compared to the theoretical value of 22,124 Dalton.
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IF anyone has any doubts or further question he's welcome to discuss it online with my professor
Did you ever post those MS which support your claims the GEP was in error, NOPE! Oh that's right the BEST SUBSTITUTE is to "talk with the prof". Damn your sickening and wasting everyones time K.
I suppose you are also going to deny you sent me a PM that clearly stated your GH had an R&D connection! Shall I post that one or do I need to "speak with your prof".