Large Scale Isolation, Characterization and Classification of Pig Immunoglobulin κ-Chains.

The ℵ-chains were prepared by chromatography and rechromatography of pig S-sulfoimmunoglobulin on Sephadex G-100 and SE-Sephadex, and characterized by starch-gel electrophoresis, amino acid analysis, molecular weight (25 000 ± 2500) and N-terminal amino add (alanine). From the tryptic digest of the ℵ-chains, the N-terminal tetracosapeptide was isolated and its amino acid sequence determined as Multiples equation(s) cannot be represented by ASCII text. These results provide evidence of the similarity between pig immunoglobulin ℵ-chains and the human and mouse type K Bence-Jones proteins. [ABSTRACT FROM AUTHOR]