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• W1920490622 abstract "The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase, comprising 363 residues, was determined. The sequence was deduced by automated sequencing of CNBr-cleavage, o-iodosobenzoic acid-cleavage, trypsin-digest and staphylococcal-proteinase-digest fragments. Comparison of the sequence with other class I aldolase sequences shows that the mammalian muscle isoenzyme is one of the most highly conserved enzymes known, with only about 2% of the residues changing per 100 million years. Non-mammalian aldolases appear to be evolving at the same rate as other glycolytic enzymes, with about 4% of the residues changing per 100 million years. Secondary-structure predictions are analysed in an accompanying paper [Sawyer, Fothergill-Gilmore & Freemont (1988) Biochem. J. 249, 789-793]." @default.
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• W1920490622 date "1988-02-01" @default.
• W1920490622 modified "2023-09-23" @default.
• W1920490622 title "The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase" @default.
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• W1920490622 doi "https://doi.org/10.1042/bj2490779" @default.
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