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Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.

ABSTRACT: 1. A new method is described for ;fingerprinting' cysteic acid peptides derived from the disulphide bridges of proteins. Cystine peptides are separated by paper electrophoresis and oxidized on paper by performic acid vapour. Electrophoresis at right angles to the first direction produces parallel groups of cysteic acid peptides lying off a diagonal. This ;fingerprint' reveals the way in which the cysteic acid peptides were originally joined in the protein. 2. The method allows a very easy selective purification of cysteic acid peptides. 3. By applying this method to bovine chymotrypsinogen A, we found that the half-cystine residues were linked 1-122, 42-58, 136-201, 168-182 and 191-220.

SUBMITTER: Brown JR

PROVIDER: S-EPMC1270086 | biostudies-other | 1966 Oct

REPOSITORIES: biostudies-other

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The disulphide bridges of bovine chymotrypsinogen B.

Project description:The five cystine peptides of chymotrypsinogen B have been isolated as pairs of cysteic acid peptides by the diagonal electrophoretic technique of Brown & Hartley (1963, 1966). The sequences of these peptides have been shown to be very similar to those of chymotrypsinogen A, and indicate that both zymogens have the same pattern of disulphide bridges. The determination of the sequence of residues 14-21 in chymotrypsinogen B has shown that residue 18 differs in the chymotrypsinogens from the corresponding residue in trypsinogen. Eight differences between chymotrypsinogens A and B are found in sequences accounting for 72 of the 245 residues.

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Determination of ionization constants by paper electrophoresis.

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Comment on Wang's paper on the covalent Cys-X-Lys bridges.

Project description: Not available

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The disulphide bridges of a mouse immunoglobulin G1 protein.

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