This report describes the development of novel wired chip devices for μ-HPLC analyses. The monolithic capillary column to be wired was prepared using a tri-functional epoxy monomer, tris(2,3-epoxypropyl)isocyanurate with a diamine, 4-[(4-aminocyclohexyl)methyl]cyclohexylamine. The prepared column was evaluated by SEM observation of the sectional structure of column and μ-HPLC. In addition, the reproducibility in the preparation of long capillary columns having nearly 1 m length was extensively examined for applications of novel wired chip devices. The authors demonstrated that the monolithic structure of the prepared long capillary could be finely controlled under the strictly maintained operational conditions and thus the relative standard deviation (RSD) of the column properties such as the number of theoretical plates, retention factor, and permeability could be well controlled to become less than 10%. Furthermore, the wired chip device column showed that its high performance was kept even after chip preparation.

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Human plasma contains a cell-adhesive protein that has a structure related to immunoglobulins. This protein was purified by affinity chromatography on an elastin-Sepharose column and by Mono Q anion-exchange chromatography. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis under non-reducing and reducing conditions revealed that this protein is a kind of immunoglobulin M (IgM). Antibodies against the mu chain and against the Fc region of IgM inhibited the adhesion of cells to this protein. Addition of the peptide GRGDS into media inhibited the adhesion, too. These results suggest that this protein is a special subset of IgM having a cell-binding sequence in the Fc region. We propose the name "cell-adhesive immunoglobulin M (CA-IgM)" for this protein. CA-IgM binds to alpha-elastin and laminin suggesting that it may play a role in the interaction between cells and the extracellular matrix.