These results suggest that prestin subunits are individually functional within a given multimer.

VWF multimer patterns were evaluated in baseline serum samples by gel electrophoresis followed by Western blotting.

The average multimer size of vWF produced endogenously by human umbilical vein endothelial cells was similarly reduced following secretion.

First, oxidation of these residues leading to the formation of intermolecular disulfide bonds results in formation of stabilized multimer.

The average multimer size of plasma VWF in TSP-1 null mice was significantly smaller than in wild type mice.

Significantly, platelet VWF multimer size was reduced upon lysis or activation of wild type murine platelets but not TSP-1 null platelets.

In addition, the multimer size of VWF released from endothelium in vivo was reduced more rapidly in TSP-1 null mice than in wild type mice.

Under non-reducing conditions the chains formed multimers of about 200 kDa.

Selective loss of high molecular weight multimers was seen only in a minority of patients.

The results indicate that FliG has a significant tendency to form multimers independently of other flagellar components.

We present a plasmid-based system in which upstream trans-splicing efficiently generates mRNAs that encode head-to-tail protein multimers.

Only the large vWF multimers are effective in promoting platelet adhesion to a site of vascular injury.

The tandem multimers assembled into CRAC channels, as seen by rectifying inward currents and by cytoplasmic calcium elevations.

Southern blotting revealed a ladder composed of DNA fragments that were multimers of the 300-bp Hinf I band.

However, mobilization of the P-element transposons containing ACE3 multimers results in deletions within the array at a high frequency.

In the shear force of flowing blood, however, only the very large VWF multimers are effective in capturing platelets.