Sentence examples for molecular mass shift from inspiring English sources

The elution volume of the monomer decreased upon binding FADox and FADred resulting in an apparent molecular mass shift of about 2 4 kDa.

The lack of molecular mass shift for these three membrane-integrated proteins (i.e., when compared to the size of their translation products alone [lane 1]) also confirmed that each protein is devoid of a cleavable transit peptide.

Additionally, there was no molecular mass shift in the β-subunit of phycocyanin of the complemented strain on SDS-PAGE visible.

The elution volume for the 7B2 peak was reproducibly shifted by 1.8 mL, corresponding to an upward molecular mass shift of ∼20 kDa, when a higher concentration of the protein was applied to the gel filtration column.

We further confirmed that Asn 540 is not utilized for glycosylation by digesting the WT and 3-Mut (with Asn 240, Asn 339, and Asn 754 mutated to Ala) with PNGase F. The results indicate that there is no additional molecular mass shift of 3-Mut after PNGase F treatment and that 3-Mut migrates like WT hTfR2 digested with PNGase F on SDS PAGE gels.

A higher molecular mass shifted the brittle-to-ductile transition towards lower temperatures.

Treatment of the bicyclic peptides with the thiol-alkylating iodoacetamide resulted in a 57 Da increase in molecular mass and shift of the peptide retention time for the product of the cStrep3(C -Z3C preC -Z3C precursorut not for that of cStreprotein3C, which is consistent with the presence of a free thiol from (from IntC+1 cysteine) in the former but not in the latter.

As previously shown [16], resting cells showed a 2 3 fold higher SN/P ratio when compared to activated cells, confirming that A3G in resting T cells is prevalently in a low molecular mass form that shifts to a high molecular mass complex when cells are activated.

With silibinin and tunicamycin cotreatment, the molecular mass of ICAM-1 shifted from approximately 72 kDa to approximately 55 kDa.

With the prolonged incubation of silibinin-treated cell lysates with PNGase F, the expression of the smaller molecular mass of ICAM-1 shifted from 72 kDa to 55 kDa, similar to the effects of tunicamycin.

Several posttranslational modifications, e.g. N-glycosylation, proteolysis, C-mannosylation and palmitoylation, might lead to the significant shift in molecular mass of about 9 kDa and give rise to different forms of CD95.