TY - JOUR
T1 - Immunocytochemical localization of vigilin, a tRNA-binding protein, after cell fractionation and within the exocrine pancreatic cell of the rat
AU - Klinger, Matthias H.F.
AU - Kruse, Charli
N1 - Funding Information:
Acknowledgements. The skilful work of Kerstin Fibelkorn, Emel Klink, and Sonja Markmann is gratefully acknowledged. This work was supported by the Deutsche Forschungsgemeinschaft (DFG - Kr 151211-1).
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 1996
Y1 - 1996
N2 - A polyclonal antibody against a fusion protein composed of two vigilin domains and γ-galactosidase was used to localize the tRNA-binding protein vigilin at the ultrastructural level. Immunoreactivity for vigilin was found on membranes bearing ribosomes within the microsome fraction derived from rat livers and on the rough endoplasmic reticulum in rat exocrine pancreatic cells, thus corroborating the involvement of vigilin in protein synthesis. Gold labeling was also found in the nucleus and in the microsome fraction in an osmiophilic substance resembling heterochromatin. Both of these localizations, the rough endoplasmic reticulum and the nucleus, are in line with the observation that a vigilin-containing ribonucleoprotein complex binds tRNA.
AB - A polyclonal antibody against a fusion protein composed of two vigilin domains and γ-galactosidase was used to localize the tRNA-binding protein vigilin at the ultrastructural level. Immunoreactivity for vigilin was found on membranes bearing ribosomes within the microsome fraction derived from rat livers and on the rough endoplasmic reticulum in rat exocrine pancreatic cells, thus corroborating the involvement of vigilin in protein synthesis. Gold labeling was also found in the nucleus and in the microsome fraction in an osmiophilic substance resembling heterochromatin. Both of these localizations, the rough endoplasmic reticulum and the nucleus, are in line with the observation that a vigilin-containing ribonucleoprotein complex binds tRNA.
UR - http://www.scopus.com/inward/record.url?scp=0029856204&partnerID=8YFLogxK
U2 - 10.1016/S0940-9602(96)80086-0
DO - 10.1016/S0940-9602(96)80086-0
M3 - Journal articles
C2 - 8817039
AN - SCOPUS:0029856204
SN - 0940-9602
VL - 178
SP - 331
EP - 335
JO - Annals of Anatomy
JF - Annals of Anatomy
IS - 4
ER -