B. 1.

In a typical structure, describe and characterize the ff:

Fab Portion
Digestion with papain breaks the immunoglobulin molecule in the hinge region before the H-H inter-chain disulfide bond Figure 4. This results in the formation of two identical fragments that contain the light chain and the VH and CH1 domains of the heavy chain. Antigen binding - These fragments were called the Fab fragments because they contained the antigen binding sites of the antibody. Each Fab fragment is monovalent whereas the original molecule was divalent. The combining site of the antibody is created by both VH and VL. An antibody is able to bind a particular antigenic determinant because it has a particular combination of VH and VL. Different combinations of a VH and VL result in antibodies that can bind a different antigenic determinants.

Fc Portion
Digestion with papain also produces a fragment that contains the remainder of the two heavy chains each containing a CH2 and CH3 domain. This fragment was called Fc because it was easily crystallized.

Heavy and Light Chains All immunoglobulins have a four chain structure as their basic unit. They are composed of two identical light chains (23kD) and two identical heavy chains (50-70kD) Variable (V) and Constant (C) Regions
When the amino acid sequences of many different heavy chains and light chains were compared, it became clear that both the heavy and light chain could be divided into two regions based on variability in the amino acid sequences. These are the: 1. Light Chain - VL (110 amino acids) and CL (110 amino acids) 2. Heavy Chain - VH (110 amino acids) and CH (330-440 amino acids)

Hinge Region
This is the region at which the arms of the antibody molecule forms a Y. It is called the hinge region because there is some flexibility in the molecule at this point.

2. Enumerate at least 3 methods of how antibody can be studied and tested and describe.

Transfusion reaction

Human blood is typed by certain markers (called antigens) on the surface of red blood cells If you get a blood transfusion, the transfused blood must match your type; that is, it must have the same antigens as your red blood cells. If you get a transfusion of blood with antigens different from yours (incompatible blood), yourimmune system destroys the transfused blood cells. This is called a transfusion reaction and can cause serious illness or even death. This is why matching blood type is so important. Rh sensitization

Rh is an antigen. The full name for this antigen is Rhesus factor. If a pregnant woman with Rh-negative blood is pregnant with a baby (fetus) with Rhpositive blood, Rh sensitization may occur. The baby may have Rh-positive blood if the father has Rh-positive blood. Rh sensitization happens when the baby's blood mixes with the mother's blood during pregnancy or delivery. This causes the mother's immune system to make antibodies against the baby's red blood cells in future pregnancies. This antibody response is called Rh sensitization and, depending on when it happens, can destroy the red blood cells of the baby before or after it is born. If sensitization happens, a fetus or newborn can develop mild to severe problems (called Rh disease or erythroblastosis fetalis). In rare cases, if Rh disease is not treated, the fetus or newborn may die. A woman with Rh-negative blood can get a shot of Rh immunoglobulin (such as RhoGAM) that almost always stops sensitization from occurring. Problems from Rh sensitization have become very rare since Rh immunoglobulin was developed.
Direct Coombs test

The direct Coombs test finds antibodies attached to your red blood cells. The antibodies may be those your body made because of disease or those you get in a blood transfusion.

3. What are the properties of an antibody? ONE COMMON DEFINING PROPERTY OF ANTIBODIES: ALL ANTIBODIES EXHIBIT SPECIFIC BINDING TO ANTIGEN Different antibodies may show various combinations of effects; some antibodies may

precipitate but not interact with complement (and therefore not show cytolysis), some may be opsonizing but not be capable of agglutination. The single common feature of all antibodies, however, is that of specific recognition and binding to antigen. All other effects, physical or biological, are secondary consequences of this specific binding.

The variable region of antibodies is formed by spicing together different short segments of DNA during the maturation of the B cell. Using this mechanisms, millions of different variable regions, and thus different antibodies can be made. Antibodies bind to antigens by attractive forces and complementary (key-in-lock) shapes. Antibodies help defend against pathogens by activating complement, serving as opsonins, agglutinating and sterically hindering pathogens and by neutralizing toxins.

Antibodies, also called immunoglobulins, are large Y-shaped proteins which function to identify and help remove foreign antigens or targets such as viruses and bacteria. Every different antibody recognizes a specific foreign antigen. This is because the two tips of its Y a re specific to each antigen, allowing different antibodies to bind to different foreign antigens. Antibodies are produced by the immune system in response to the presence of an antigen. Antigens are large molecules, usually proteins, on the surface of cells, viruses, fungi, bacteria, and some non-living substances such as toxins, chemicals, and foreign particles. Any substance capable of triggering an immune response is called an antigen.
Antibodies are a class of proteins that are generated by the immune system to neutralize foreign pathogens such as bacteria, fungi and viruses. Although the general structures of different antibodies are very similar, only the relatively small variable regions, located near the tip of the protein, are involved in the binding of an antibody to a particular target, or antigen. Within these variable regions are six hypervariable regions, also known as complementarity determining regions (CDRs). The diversity contained within these CDRs represents a significant portion of the overall diversity amongst antibodies, and is responsible for the ability of otherwise structurally similar antibodies to specifically bind vastly different antigens.