期刊名称:Proceedings of the National Academy of Sciences
印刷版ISSN:0027-8424
电子版ISSN:1091-6490
出版年度:1972
卷号:69
期号:12
页码:3689-3692
DOI:10.1073/pnas.69.12.3689
语种:English
出版社:The National Academy of Sciences of the United States of America
摘要:Fab-fragments of several phosphorylcholine-binding mouse-myeloma proteins have been prepared by pepsin digestion; two of these, MOPC 167 and McPC 603, gave large crystals from ammonium sulfate solutions. The Fab-fragment from MOPC 167 crystallizes in a hexagonal space group, but does not diffract to a resolution greater than about 8 A. In contrast, McPC 603 crystals (space group P63) diffract to about 2.7 A. An isotopic double-labeling technique was developed that demonstrated that the 603 crystals bind 1 mol of hapten per mol of Fab-fragment, but with a binding constant significantly lower than that observed in solution. The findings indicate that a three-dimensional model of this homogeneous antigen-binding immunoglobulin can be constructed. Accordingly, a search for heavy-atom derivatives and determination of the primary structure are in progress.