Figure 4.
Fig. 4. The carboxyl terminus of both CAP and MCH1 binds
actin. A, full-length MCH1 and CAP bind actin. Lysates from cap cells
(SKN50) expressing either Myc-tagged CAP or Myc-tagged MCH1 were
subjected to immunoprecipitation with anti-Myc antibody (9E10).
Specific protein interactions were blocked by the addition of
excess Myc peptide (50 µg). Immune complexes were resolved
on SDS-acylamide gels and transferred to nylon membranes.
Immunoblots were probed with an anti-actin monoclonal antibody
(20 µg/ml) (Boehringer Mannheim). B, the carboxyl-terminal
domain of CAP and MCH1 binds actin. Lysates from cap cells
expressing various Myc-tagged domains of CAP, or the
carboxyl-terminal of MCH1, were subjected to
immunoprecipitation. Immunoblots were incubated with an
anti-actin monoclonal antibody (20 µg/ml). Antigen
detection was performed by ECL chemiluminescent assay.
cap cells
(SKN50) expressing either Myc-tagged CAP or Myc-tagged MCH1 were
subjected to immunoprecipitation with anti-Myc antibody (9E10).
Specific protein interactions were blocked by the addition of
excess Myc peptide (50 µg). Immune complexes were resolved
on SDS-acylamide gels and transferred to nylon membranes.
Immunoblots were probed with an anti-actin monoclonal antibody
(20 µg/ml) (Boehringer Mannheim). B, the carboxyl-terminal
domain of CAP and MCH1 binds actin. Lysates from