Studies on humans secretory IgA comparative studies of the IgA-bound secretory piece and the free secretory piece protein

Autor: Kunihiko Kobayashi
Rok vydání: 1971
Předmět:
Zdroj: Molecular Immunology. 8:785-790
ISSN: 0161-5890
DOI: 10.1016/0161-5890(71)90055-1
Popis: Human colostral IgA was isolated and characterized for its immunological and physicochemical properties. The colostral IgA has a molecular weight fo 385,000, with a sedimentation coefficient, 11·50 S and a diffusion coefficient, 2·66. Reduction and alkylation split the colostral IgA into fragments corresponding to a serum type IgA and a secretory piece. The colostral IgA consists of two molecules of serum type IgA (mol. wt. 159,000) and one molecule of secretory piece (SP) (mol. wt. 75,500). The SP binding to IgA molecules was isolated from reduced and alkylated colostral Iga by gelfiltration followed by immunoadsorbent absorption. The isolated SP (‘bound’ SP) was homogeneous immunologically and ultracentrifugally. Normal human colostrum contained ‘free’ SP in a form unbound to IgA molecules. The ‘free’ SP was also isolated from normal human by ion-exchanged cellulose chromatiography and gelfiltration. Comparing the properties of the isolated ‘bound’ and ‘free’ SP, it was shown that they were identifical, having the same sedimentation coefficient, molecular weitht, amino acid composition and antigenic characteristics. The ‘free’ SP was further characterized for the chemical properties of its carbohydrate, sulfur and nitrogen. The SP is a glycoprotein containing a total carbohydrate of approximately 15 per cent.
Databáze: OpenAIRE