Details

Autor(en) / Beteiligte

• Komar, R.
• Abson, E.C.
• Mukkur, T.K.S.

Titel

Isolation and characterization of immunoglobulin A (IgA) from bovine nasal secretions

Ist Teil von

• Immunochemistry (1965), 1975-04, Vol.12 (4), p.323-327

Ort / Verlag

England: Elsevier B.V

Erscheinungsjahr

1975

Quelle

MEDLINE

Beschreibungen/Notizen

• IgA was found to exist in two polymeric forms (15·3S and 12·2S) in bovine nasal secretions. The 15·3S secretory IgA (S-IgA)† dissociated into 12·2S and 7S components and a trailing edge upon treatment with 4 M Guanidine-HCl. The partial specific volume ( v ) and molecular weight of the 12·2S IgA were calculated to be 0·721 g/cc and 430,380 g/mole respectively. The mol. wt of the 15·3S polymer was determined to be 642,000 g per mole assuming a v of 0·721 g/cc. The 12·2S S-IgA was found to show complete identity with the 15·3S S-IgA and in addition shared antigenic determinants with human colostral IgA. J-chain was released from both species of S-IgA following treatment with 2-mercaptoethanol. The molecular weight of J-chain from S-IgA (Jα) was determined to be 17,040 by SDS-PAGE. Antigenic analysis showed J α and J μ (bound-form) to be identical. Stoichiometric studies of J-chain determined from densitometric scans of polyacrylamide gels of reduced and alkylated bovine 12·2S S-IgA revealed the presence of one J-chain per S-IgA molecule.