The Complete Amino-Acid Sequence of the Heavy Chain of the Human Myeloma Protein WIE, an Immunoglobulin D

Abstract

The human myeloma protein WIE is achains, O-glycosylations are confined to the hinge retype immunoglobulin D; the amino-acid sequence of gion. Furthermore, the ratios of 7V-glycosylations at its Fc part and aminoethylated heavy chain was comthe three positions are identical in IgD WAH pletely determined. The V H -part (subgroup III) be- [Takahashi, N. et al. (1984) /. Chromatogr. 317, gins W-terminally with 5-oxoproline, and it contains a 11-26.] and IgD WIE (100%, 50%, 100% ). long, unique CDR3 region. Since the constant part From the most conserved constant domain, C53, a differs from known chains by one amino-acid subthree-dimensional model was constructed to clarify stitution in the hinge region, IgD WIE probably repre-the role of its o. sp ecific substitutions and glycosylasents an allotypic variant. As in other protein t i on Die vollständige Aminosäure-Sequenz der schweren Kette des menschlichen Myelomproteins WIE, einem Immunglobulin D Zusammenfassung: Das menschliche Myelomproethylierten schweren (H-) Kette wurde vollständig ertein WIE ist ein Immunglobulin D vom -Typ; die mittelt. Der variable Teil aus der Subgruppe III beAminosäure-Sequenz vom Fc-Teil und der aminoginnt mit einem 5-Oxoproline-Rest und enthält eine Enzymes: Serine carboxypeptidase, peptidyl-L-amino-acid hydrolase (EC 3.4.16.1) (also named carboxypeptidaseY); Carboxypeptidase A, peptidyl-L-amino-acid hydrolase (EC 3.4.17.1);