N-ethylmaleimide sensitive fusion protein (NSF) and soluble NSF attach
ment proteins (SNAPs) are involved in many vesicular transport steps.
It has been proposed that SNAPs and NSF associate with their membrane
receptors only when vesicles dock on the target membrane. Analysis of
NSF and alpha-SNAP distribution in fractionation of organelles from ad
renal medulla indicated that a substantial amount of both proteins dis
tributed with chromaffin granules. Further fractionation of intact gra
nules and lysed granule membranes showed exact overlap of NSF and alph
a-SNAP distribution with chromaffin granules. These results suggest th
at NSF and alpha-SNAP are associated with chromaffin granules and supp
ort the idea that they function prior to docking of the granules on th
e plasma membrane. (C) 1997 Federation of European Biochemical Societi
es.