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The dominant enamelins in secretory-stage rat enamel migrated at around 60 70 kDa.
In contrast, the dominant enamelins in secretory-stage porcine enamel migrated at around 32 kDa.
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As shown in Western blots of culture supernatants from the rSAK-2 strain, a single well-defined band at around 16 kDa that migrated parallel to that of E. coli-produced rSAK-1 (ThromboGenics NV) is present.
Populations isolated from around the world, migrated at angles to the magnetic vector that would optimize vertical translation in their native soil, with northern- and southern-hemisphere worms displaying opposite migratory preferences.
Because of their amphiphilic character, inisurfs migrated at oil/water interface and initiated polymerization from bromoisobutyryl ester groups.
Three bands were identified using this antibody in PNM preparations that migrated at 28, 33 35 and 62 64 kDa.
However, a high molecular weight IK1 complex that migrated at >220 kDa was present (Fig. 6A).
Here, we detected one clear band that migrated at approximately 5 kb.
The unglycosylated mutant migrated at 60 kDa, corresponding to the polypeptide mass (Fig. 2B).
In accordance with the results for endogenous ERp90 we found that myc-ERp90 migrated at ∼95 kDa (Figure 5B).
A band that migrated at 195 kDa was seen using the antibody for PDGFRα.
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