- A novel quadripartite dsRNA virus isolated from a
- DS-215N - Essae
- Mass Spectrometric Analysis of 40 S Ribosomal Proteins from Rat-1
- DS-425 - Rice Lake Wehing Systems
A novel quadripartite dsRNA virus isolated from a
S2, S3, S9, S10, S12, S14, and S25 showed changes in mass inconsistent with known covalent modifications ( 220, −75, 86, 56, −100, −117, and −103 Da, respectively), possibly representing novel post-translational modifications or allelic sequence variation.
DS-215N - Essae
Although sequences of most mammalian ribosomal proteins are available, little is known about the post-translational processing of ribosomal proteins.
Mass Spectrometric Analysis of 40 S Ribosomal Proteins from Rat-1
To examine their post-translational modifications, 40 S subunit proteins purified from Rat-1 fibroblasts and their peptides were analyzed by liquid chromatography coupled with electrospray mass spectrometry.
DS-425 - Rice Lake Wehing Systems
Of 41 proteins observed, 36 corresponded to the 32 rat 40 S ribosomal proteins with known sequences (S3, S5, S7, and S24 presented in two forms).
Teraoka scale ds-425 manual:
Rating: 98 / 100
Overall: 94 Rates