drake10 - Immunoglobulins as Binding Proteins Lecture 10,...

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Immunoglobulins as Binding Proteins Lecture 10, Medical Biochemistry
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Lecture 10, Outline Structures of Immunoglobulins Functional and Structural Differences between class members The immunoglobulin fold motif in immunoblobulins and other binding proteins
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Immunoglobulin Function The primary function of immunoglobulin molecules are to bind "foreign" proteins, carbohydrates, nucleic acids and glycolipids so that they can be cleared from the organism by cells specialized to perform such processes. Immunoglobulins typically bind antigens with K d values in the picomolar to micromolar range. As part of this function, immunoglobulins are found in extracellular fluids, a variety of bodily secretions, and attached to the outer surface of cell membranes
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Immune System Overview
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Each immunoglobulin has two binding sites
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Immunoglobulin Structure Immunoglobulins consist of two types of polypeptides, H chains for "heavy" molecular weight and L chains for “light” molecular weight.
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Bence-Jones Proteins Structures of immunoglobulins (IG) were first deduced using "Bence-Jones" proteins (IG molecules) isolated from urine and plasma of patients with multiple myeloma. In this disease, a single B lymphocyte proliferates uncontrollably and develops into a large clonal pool of essentially
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drake10 - Immunoglobulins as Binding Proteins Lecture 10,...

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