Open AccessAmino Acid Sequence around Disulfide Bridge of Pig Immunoglobin λ‐Chains
Author(s) -
Franěk F.,
Keil B.,
Nvotný J.,
ŠOrm F.
Publication year - 1968
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1967.tb19548.x
Subject(s) - chemistry , sephadex , size exclusion chromatography , disulfide bond , yield (engineering) , cystine , formic acid , chromatography , peptide , peptide sequence , amino acid , antibody , pepsin , biochemistry , bence jones protein , cysteine , immunoglobulin light chain , biology , enzyme , materials science , immunology , metallurgy , gene
The λ‐chains of normal pig γG‐immunoglobulin were digested with pepsin in 1 M formic acid. Cystine‐containing peptides were isolated by gel filtration on Sephadex G‐25 and by chromatography on Dowex 50 and Dowex 1. The following structures were found:In addition to these peptides obtained in a high yield similar peptides were found but their complete structures were not determined in view of their low yield. The structures found in the λ‐chains display a high degree of similarity with corresponding structures known to exist in human Bence‐Jones proteins of the l ‐type.