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- W2095324673 abstract "Abstract A disulfide bridge formed at the active site of rabbit muscle aldolase has now been shown to involve specific cysteine residues in the NH 2 - and COOH-terminal regions of the molecule. A new peptide, containing one of these cysteine residues, has been isolated from the NH 2 -terminal BrCN peptide (peptide N), bringing the total number of cysteine-containing peptides in the aldolase subunit to 8. The distribution and reactivity of the 8 sulfhydryl groups permits some deductions regarding the manner in which the peptide chain is folded to yield the three-dimensional structure and to form the active site." @default.
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- W2095324673 date "1971-12-01" @default.
- W2095324673 modified "2023-09-25" @default.
- W2095324673 title "The number, distribution and functional implication of sulfhydryl groups in rabbit muscle aldolase" @default.
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- W2095324673 doi "https://doi.org/10.1016/0006-291x(71)90189-6" @default.
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