The isolation and properties of a fragment of bovine-serum albumin which retains the ability to combine with rabbit antiserum
- 1 August 1957
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 66 (4) , 677-686
- https://doi.org/10.1042/bj0660677
Abstract
Chymotryptic digestion of bovine - serum albumin in a dialysis sac produced a diffusible digestion product which retained the power to combine with rabbit antibovine-serum albumin. This product was isolated, principally by zone electrophoresis. The N-terminal amino acid is phenylalanine. The molecular weight of the active fragment is about 12,000, but it readily dimerizes, probably through a free sulfhydryl group. The reaction of this substance with different rabbit antisera was studied and the results used to classify the different types of antibody which appear to be present in all antisera. This active fragment can provoke anaphylactic shock in a guinea pig passively immunized by injection of rabbit anti-bovine-serum albumin.Keywords
This publication has 16 references indexed in Scilit:
- CHROMATOGRAPHY OF AMINO ACIDS ON SULFONATED POLYSTYRENE RESINSPublished by Elsevier ,2021
- Methodological studies of zone-electrophoresis in vertical columnsBiochimica et Biophysica Acta, 1956
- [Study of the degradation of human serum albumin by rabbit spleen extract. II. Demonstration of three different specific groupings in the antigenic pattern of human albumin and of three corresponding antibodies in rabbit antihuman-albumin serum].1955
- The fractionation of rabbit γ-globulin by partition chromatographyBiochemical Journal, 1955
- CRYSTALLINE PAPAIN .1. PREPARATION, SPECIFICITY, AND ACTIVATION1954
- Ultraviolet Absorption Spectra of Proteins and Amino AcidsAdvances in Protein Chemistry, 1952
- THE CRYSTALLIZATION AND SEROLOGICAL DIFFERENTIATION OF A STREPTOCOCCAL PROTEINASE AND ITS PRECURSORThe Journal of Experimental Medicine, 1950
- The formation of a specific inhibitor by hydrolysis of rabbit antiovalbuminBiochemical Journal, 1950
- Preparation of Crystals Containing Protease from Aspergillus oryzæNature, 1950
- PROTEIN MERCAPTIDESCold Spring Harbor Symposia on Quantitative Biology, 1950