Ultrastructural localization of actin in nuclear matrices from mouse leukemia L5178Y cells.
We examined the distribution of actin in isolated nuclear matrices from mouse leukemia L5178Y cells using an anti-actin antibody and protein A-conjugated colloidal gold particles. Before immunogold staining, we partially digested the surface lamina of the nuclear matrix with trypsin (Nakayasu and Ueda, Exp. Cell Res. 143, 55-62, 1983) to allow penetration of the gold particles into the nuclear matrix. Trypsin digestion slightly modified the internal structure of the nuclear matrix, but did not affect the actin content in the nuclear matrix nor the reactivity of actin with the antibody. Many colloidal gold particles were present along fibrogranular structures in the nuclear matrix. The results reported here confirm the existence of actin in the interior of the nuclear matrices of L5178Y cells.
Nakayasu
H
H
Ueda
K
K
D000199:Actins / Q000032:analysis*; D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000032:analysis* / Q000648:ultrastructure; D003593:Cytoplasm / Q000032:analysis / Q000648:ultrastructure; D004797:Enzyme-Linked Immunosorbent Assay; D006046:Gold; D007940:Leukemia L5178 / Q000473:pathology*; D007942:Leukemia, Experimental / Q000473:pathology*; D051379:Mice; D013194:Staining and Labeling; D014357:Trypsin
D000199:Actins; D006046:Gold; D014357:Trypsin