The primary structure of the basic isoform of Acanthamoeba profilin.
Acanthamoeba profilin-II [Kaiser, D.A., Sato, M., Ebert, R. F. and Pollard, T.D. (1986) J. Cell. Biol. 102, 221-226] was digested with trypsin or cleaved by 2-(2-nitrophenylsulphenyl)-3-methyl-3-bromoindolenine. The tryptic peptides were purified by reversed-phase-high-performance liquid chromatography and completely sequenced using automated gas-phase sequence analysis. The complete profilin-II sequence was deduced by ordering the tryptic peptides using the sequence information of the tryptophan-cleavage products. Acanthamoeba profilin-II was found to be homologous to the previously determined profilin-I sequence [Ampe, C., Vandekerckhove, J., Brenner, L., Tobacman, L. and Korn, E.D. (1985) J. Biol. Chem. 260, 834-840]. Like profilin-I, profilin-II consists of 125 amino acids, has a blocked NH2 terminus and a trimethyllysine residue at position 103. Profilin-II differs in at least 21 positions from one of the profilin-I isoforms. The amino acid exchanges are mainly concentrated in the middle part of the sequence. Profilin-II contains two more basic residues than profilin-I, which explains its higher isoelectric point.
Ampe
C
C
Laboratory of Genetics, State University Ghent, Belgium.
Sato
M
M
Pollard
T D
TD
Vandekerckhove
J
J
D000048:Acanthamoeba / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003285:Contractile Proteins; D008840:Microfilament Proteins / Q000302:isolation & purification; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D051304:Profilins; D014357:Trypsin
D003285:Contractile Proteins; D008840:Microfilament Proteins; D010446:Peptide Fragments; D051304:Profilins; D014357:Trypsin