Proprotein processing within secretory dense core granules oftetrahymena thermophila *

HIGHLIGHTS

• who: Niels R. Bradshaw from the to secrete with , mM dibucaine, and the secreted material was purified. In the final step, the secreted protein was centrifuged at, ⫻ g for , min to yield a flocculent pellet whose volume was estimated. ␤-Mercaptoethanol was added to, %, and the sample was heated at , °C for , min. Under these conditions, virtually all mature Grl1p remains soluble, whereas most other polypeptides form aggregates [2]. Samples were centrifuged at, ⫻ g for , min, and the supernatants were subjected to SDS-PAGE (15% polyacrylamide, .09% bisacrylamide) and transferred to polyvinylidene difluoride (Osmonics, Westboro, MA). The strong . . .
  

   

  

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