THIOL AND DISULPHIDE CONTENTS OF HEN OVALBUMIN - C-TERMINAL SEQUENCE AND LOCATION OF DISULPHIDE BOND
THIOL AND DISULPHIDE CONTENTS OF HEN OVALBUMIN - C-TERMINAL SEQUENCE AND LOCATION OF DISULPHIDE BOND
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DOI:
10.1042/bj1160555
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发表时间:
1970-01-01
影响因子:
4.1
通讯作者:
FOTHERGI.JE
中科院分区:
文献类型:
--
作者:
FOTHERGI.LA;FOTHERGI.JE
1. The thiol and disulphide contents of hen ovalbumin were investigated byp-chloromercuribenzoate titration, by determination of cysteic acid content after performic acid oxidation, by measurement of uptake of radioactive iodoacetic acid, and by assay ofS-aminoethylcysteine after reaction with ethyleneimine. All results showed that ovalbumin had 6 half-cystine residues. Experiments with and without reducing agents demonstrated that there were 4 thiol groups and 1 disulphide bond. 2. A peptide containing equimolar amounts ofS-carboxymethyl-cysteine, serine, valine and proline, but no lysine or arginine, was obtained by radioactive labelling of the cysteine residues with iodo[14C]acetic acid followed by electrophoretic and chromatographic separation of tryptic digests. It was concluded that theC-terminal sequence of ovalbumin is -Cys-Val-Ser-Pro. 3. The location of the disulphide bond was studied by using a double-labelling technique. It was shown that one end of the disulphide was located in thisC-terminal peptide.