Figure 1.

Amino acid sequencing of an 80-kD protein isolated with a pan dynamin antibody revealed strong sequence similarity to the dynamin family. An 80-kD protein recognized by the pan dynamin antibody MC12 was isolated by large scale immunoprecipitation from rat liver homogenate. The immunoprecipitate was run on a 5–15% polyacrylamide gradient gel, and the 80-kD protein band was excised and eluted from the gel. Amino acid sequencing of six tryptic peptides was conducted and compared with rat dynamins I, II, and III as well as Vps1p and Dnm1p. Peptides A to E aligned with the NH₂-terminal region of the dynamins, Vps1p and Dnm1p, and peptide F aligned with the COOH terminus of these proteins. Sequence information obtained from these peptides indicated that this protein was strongly related to the dynamins, yet different enough to represent a novel and distinct gene product. Boxes represent conserved residues.