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Figure 9.10. (a) Layout of the spotting process using solutions of HSA and BSA with different concentrations on the surface of the azopolymer. (b) Fluorescence images observed after various treatments. The left-hand side image is as observed from the spotted sample after photoimmobilization, washing, and immunological reaction. Center image is as observed from a sample treated with hydrochloric acid following the rst observation. The same immunological reaction was repeated after the acid treatment, when the right-hand side image was observed.

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wnoutrefresh() has the effect of un-touching a window. See touchwin(). A similar function, pnoutrefresh(), exists for help in updating pads. See pnoutrefresh(). The slk_noutrefresh() function is used for help in updating soft labels. See slk_noutrefresh().

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antimouse polyclonal goat antibodies as a secondary antibody to detect albumins. Fluorescence emission was only observed from the spot on which the HSA had been immobilized, as shown in Fig. 9.10b, which means that a reaction that was selective to the HSA had occurred on the antigen-immobilized surface of the azopolymer and then was detected. Next, the sample was treated with hydrochloric acid to separate the antibodies from the HSA. The authors con rmed that no uorescence emission could be observed from the substrate after the HCl treatment. They then repeated the same immunoreaction on the treated sample, such that almost the same uorescence image as that described earlier was again obtained, as shown in Fig. 9.10b (center and right). This demonstrates that biochips fabricated on an azopolymer surface can be reused.

wnoutrefresh(alpha); wnoutrefresh(beta); wnoutrefresh(gamma); doupdate();

you use System.ApplicationException as a base class. An example of a user-defined exception follows:

The three wnoutrefresh() functions update information from the three windows, alpha, beta, and gamma. Then final doupdate() function updates the terminal. These four statements are more efficient than three corresponding wrefresh() functions.

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In the next phase, the authors applied the photoimmobilization method to try to obtain protein chips, and more speci cally, an immunochip Enzyme-linked immunosorbent assay (ELISA) systems are commonly used (Karlsson et al, 1991; Voller et al, 1978) as a popular method for detecting small amounts of protein in sample solutions such as serums Although the ELISA system is an excellent method for detection of proteins, it still has some problems; it is comparatively expensive, and it is dif cult to detect proteins when small quantities of the sample solution are used The authors might be able to realize an immunochip that could act as a micro-ELISA system with the capability to deal with small quantities of sample solutions if they could succeed in immobilizing the antibodies on the substrate.

wnoutrefresh(stdscr);

using System; using System.Runtime.Serialization; namespace PatientManagementShared { [Serializable] public class InvalidPatientID: ApplicationException { public InvalidPatientID( String _message ) : base(_message) { } public InvalidPatientID(SerializationInfo info, StreamingContext context): base(info, context) {} } }

Here, the standard screen is updated to the virtual screen. A subsequent call to doupdate() will update the terminal screen.

Such an immunochip could be used to measure multiple target proteins on the same substrate simultaneously, so it has the potential to become a novel method of replacing conventional ELISA systems in the elds of biochemical indexes, diagnostic agents, and clinical inspection (Kambhampati, 2003) One can say that the photoimmobilization method is one of the most promising prospects for immunochip applications because it can provide immobilization on the substrate surface irrespective of the surface states of the biomolecules The authors rst examined speci c reactions of photoimmobilized antibodies on azopolymer surfaces for the immunochip application Solutions of anti-goat antibodies (left-hand side) and anti-rabbit antibodies (right-hand side) were spotted onto an azopolymer surface at different concentrations, the layout of which is shown in Fig 911a After photoimmobilization and washing, the sample was reacted separately with Cy-5-labeled antigens (goat IgG and rabbit IgG).

refresh(), doupdate(), wredrawln(), touchwin()

Note that the class has to provide a so-called deserialization constructor (the constructor with the SerializationInfo and StreamingContext parameters) and it has to be marked [Serializable], otherwise the marshaling will not work. The exception s body is empty, because we have no additional parameters compared to Exception.

The anti-goat IgG antibody recognized goat IgG when Cy-5-labeled goat IgG was introduced onto the sample, whereas anti-rabbit IgG recognized rabbit IgG when Cy-5-labeled rabbit IgG was introduced, as shown in Fig 911b and c The speci c reactivity of the antibodies was realized by xing photoimmobilized antibodies on the surface of the azopolymer They also examined the preservation stability of the photoimmobilized antibodies Although the reactivity of the antibodies dropped.

wredrawln()

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