Non-antigenic and Low Allergic Gelatin Produced by Specific Digestion with an Enzyme-Coupled Matrix

概要

論文の詳細を見る
Poricine gelatin (heat-denatured collagen) was digested with a bioreactor using an enzyme-coupled matrix (ECM) with purified collagenase. The diegsted gelatin, FreAlagin type R (M.W. range 200-10000 Da), was further purified by an HPLC system depending upon molecular size. The molecular weight range of the purified fractions, FreAlagin type P and type AD, were 200-500 and 2000-10000 Da, respectively, and glycine was the N-terminal amino acid of both types (≧93%). ECM has the capability of digesting gelatin at a specific point in the sequence before glycine, and it was determined that FreAlagin type P consists of a tri-peptide fraction with the amino acid sequence Gly-X-Y. No types of FreAlagin exhibited any reactivity with gelatin-specific IgC antibody raised in guinea pigs, and they also possessed an extremely low reactivity with gelatin-specific IgG antibody from the sera of patients who had experienced an anaphylactic reaction against gelatin after vaccination or after eating gelatin-containing foods. From these results, it was determined that FreAlagin types R and AD were non-antigenic, low-allergic gelatins. FreAlagin type R, and especially type AD, had strong adsorption-blocking activity comparable to the level of bovine serum albumin, whereas type P and glycine had virtually no adsorption-blocking activity. Therefore, the new types of gelatin, FreAlagin types R and AD, are suitable for pharmaceutical use to avoid gelatin allergy.
公益社団法人日本薬学会の論文
1998-04-15

Non-antigenic and Low Allergic Gelatin Produced by Specific Digestion with an Enzyme-Coupled Matrix

スポンサーリンク

概要

著者

関連論文

スポンサーリンク