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- W2091279167 abstract "An immune system, viz, heat denatured bovine serum albumin (HDBSA) and rabbit anti-HDBSA was studied to learn the nature of the antibody combining sites, Enzyme (trypsin, chymotrypsin, pepsin) digested HDBSA yielded immunologically active peptide, which were dialyzable and non-dialyzable. The peptides had molecular weights ranging from 5000 to 100,000 and showed differences in amino acid composition. The immunological activity with anti-HDBSA sera was proportional to the mol. wt. of the peptide. All active fractions, except those from peptic digests, also evoked passive cutaneous anaphylaxis (PCA) reactions in guinea pigs with antisera to native BSA. Ten to twenty times more weight of dialyzable fraction compared with non-dialyzable fraction was needed to produce equivalent inhibition of the homologous precipitin reaction and to evoke PCA reactions. Performate oxidation of HDBSA reduced immunological activity 50% and further peptic digestion abolished the ability to elicit the PCA reaction. Degradation of the trypsin resistant core of HDBSA with chymotrypsin yielded additional dialyzable peptides with molecular weights between 5000 and 10,000 having immunological activities. An immunologically active fragment of mol. wt. about 7200 was isolated from the tryptic digest. The immunological findings are consistent with the concept that HDBSA is partially extended molecule having antibody combining sites distribution among several areas on the surface rather than being restricted to one localized region." @default.
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- W2091279167 date "1967-01-01" @default.
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- W2091279167 title "Immunochemical studies of the tryptic, chymotryptic and peptic peptides of heat denatured bovine serum albumin" @default.
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- W2091279167 doi "https://doi.org/10.1016/0019-2791(67)90191-7" @default.
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