Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments.
Fructose-1,6-bisphosphate aldolase was purified from human skeletal-muscle by affinity elution chromatography. Four CNBr-cleavage fragments were purified by gel filtration, and their N-terminal amino acid sequences were determined. Cleavage with o-iodosobenzoic acid at the three tryptophan residues also yielded fragments suitable for N-terminal sequence analysis. Thus, the sequence of 272 of the 363 residues was established. These sequence results allow many of the discrepancies between the two published rabbit skeletal-muscle aldolase sequences to be resolved. The human aldolase sequence reported here is 96% identical to a "consensus" rabbit aldolase sequence. A comparison with a partial sequence of Drosophila aldolase (103 residues) shows 80% identity. The determination of the amino acid sequence of human aldolase is important for the interpretation of the crystal structure of this enzyme.
D000595:Amino Acid Sequence; D000818:Animals; D003488:Cyanogen Bromide; D004330:Drosophila / Q000201:enzymology; D005634:Fructose-Bisphosphate Aldolase / Q000302:isolation & purification*; D006801:Humans; D007463:Iodobenzoates; D009132:Muscles / Q000201:enzymology*; D010446:Peptide Fragments / Q000302:isolation & purification*; D011817:Rabbits
D007463:Iodobenzoates; D010446:Peptide Fragments; C008154:2-iodosobenzoic acid; D005634:Fructose-Bisphosphate Aldolase; D003488:Cyanogen Bromide