title: Determination of the molecular structure of the human free secretory component.
abstract: Here, we present the experimental data, leading to determination of the primary structure, the linkage of the carbohydrates and the arrangements of the disulfide bonds of the human free secretory component. Methods of protein chemistry were used. The protein can be divided into five homology regions and is a member of the immunoglobulin superfamily.
authors.affiliation: Department of Immunochemistry, Max-Planck-Institut für Experimentelle Medizin, Göttingen.
authors.forename: H
authors.initials: H
authors.lastname: Eiffert
authors.forename: E
authors.initials: E
authors.lastname: Quentin
authors.forename: M
authors.initials: M
authors.lastname: Wiederhold
authors.forename: S
authors.initials: S
authors.lastname: Hillemeir
authors.forename: J
authors.initials: J
authors.lastname: Decker
authors.forename: M
authors.initials: M
authors.lastname: Weber
authors.forename: N
authors.initials: N
authors.lastname: Hilschmann
mesh_terms: D000595:Amino Acid Sequence; D002241:Carbohydrates / Q000737:chemistry; D002851:Chromatography, High Pressure Liquid; D003126:Colostrum / Q000737:chemistry*; D004220:Disulfides / Q000737:chemistry; D006801:Humans; D007136:Immunoglobulins / Q000145:classification; D008969:Molecular Sequence Data; D012635:Secretory Component / Q000737:chemistry*; D012689:Sequence Homology, Nucleic Acid
chemical_list: D002241:Carbohydrates; D004220:Disulfides; D007136:Immunoglobulins; D012635:Secretory Component