Immunochemistry of bovine serum albumin.
Adv Exp Med Biol
; 98: 101-17, 1978.
Article
em En
| MEDLINE
| ID: mdl-82378
ABSTRACT
Two fragments were isolated from BSA one was derived from the first terminal third of the molecule and the second from the last third of the molecule. Each fragment inhibited the reaction of BSA-anti BSA by 90% or better. An immunoabsorbent of each bound 90% of anti BSA. Each fragment bound two antibody molecules per mole of fragment. These results are explained by the concept that BSA contains repeating identical or similar antigenic determinants. Conformational non identity of various batches of BSA was revealed by reactivity of the disulfide bonds at the neutral transition. Trypsin was found to cleave GSA, PSA, and HSA to yield an immunochemically reactive fragment. At least in the case of HSA, the fragment exhibited all the immunochemical reactivity of the native protein.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Soroalbumina Bovina
Limite:
Animals
Idioma:
En
Revista:
Adv Exp Med Biol
Ano de publicação:
1978
Tipo de documento:
Article