Pulmonary embolism (PE) is a common clinical problem affecting 600,000 patients per year in the United States. Although the diagnosis can be easily confirmed by imaging techniques, such as computed tomographic angiography of the chest, the identification of underlying mechanism leading to PE is important for appropriate duration of anticoagulation, and prevention of subsequent episodes. The differential diagnosis of underlying mechanism is broad and must include careful review of medication history. Drug-related thromboembolic disease can be easily missed and may have catastrophic consequences. The identification of the culprit drug is important for prevention of subsequent episodes and choosing appropriate duration of anticoagulation. We report a case of a middle-aged man who developed PE after administration of intravenous immunoglobulin.

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The interaction between protein A and immunoglobulin G (IgG) was studied at a variety of pH values using a surface plasmon resonance (SPR) device, which provides real time kinetic data without labelling or molecular alteration. This study was carried out due to the large scale use of Protein A affinity chromatography for the purification of IgG for pharmaceutical purposes, and is one of the most costly steps in the purification process. The results produced were largely in line with those produced in previous literature with binding remaining strong between pH 7.4 and 5.0, although the association rate decreased as pH decreased. Below pH 5.0, the rate of IgG elution markedly increased, with pH 3.5 showing near full elution seconds after the association phase of the SPR interaction finished. Problems were encountered with non-specific binding between the SPR sensor chip and IgG occurring under a variety of conditions, requiring various remedies. However, no complete interactions were successfully carried out under pH 5.0, so the results obtained below this value were obtained by binding at pH 7.4 and then elution at the desired pH. The data showed binding behaviour that was most successfully explained by a three-site model, each with a binding ratio of 1:1. The binding ratio is questionable given that Protein A and IgG typically bind at a ratio of 1:2 but may be explained by the sites being independent of one another and thus no secondary attachment is observed. A variety of models were fitted to the data but only two- and three-site models fitted the experimental data, with the three-site model being a more accurate and robust fit across pH changes. A multiple site model seems intuitively correct given the six different binding sites that Protein A has for interaction with IgG. The models produced have potential applications in a larger model of Protein A affinity chromatography, although a number of additional factors would need to be taken into account, such as mass transfer effects and the IgG concentration gradient.

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by Julia Luen-wah Woo. / Thesis (M.Ph.) -- Chinese University of Hong Kong, 1988. / Bibliography: leaves 90-94.

Thesis (Ph. D.)--Brigham Young University. Dept. of Chemistry and Biochemistry, 2006. / Includes bibliographical references.

Allorecognition, defined as the ability to discriminate between self and non-self, is ubiquitous to colonial metazoans and widespread in aclonal taxa. Invertebrate allorecognition phenomena are of broad interest and have long captured the attention of geneticists by virtue of the allotypic diversity they display, marine ecologists by virtue of their control of effector mechanisms determining the outcome of intraspecific competition, evolutionary biologists by virtue of their regulation of the level at which selection acts, and immunologists by virtue of their resemblance to the allogeneic interactions that characterize pregnancy and transplantation in vertebrates. Diverse histocompatibility modes have been described in the jawed vertebrates, protochordates, and cnidarians, which are to date the only three taxa for which a genetic model to study allorecognition has been developed. Outside of the MHC-based histocompatibility of vertebrates, allorecognition determinants have been recognized in only two invertebrates. In the tunicate Botryllus, two genes involved in the histocompatibility response were characterized, FuHc and fester. In Hydractinia, the loci controlling allorecognition, alr1 and alr2, were mapped to a single chromosomal region, the allorecognition complex, and alr2 was recently identified as a polymorphic immunoglobulin superfamily (IgSF) receptor. In this study, the identification of the second Hydractinia allodeterminant, alr1, was undertaken. Chapter I briefly reviews prominent allorecognition model organisms and details the phenomenon in the model organism, Hydractinia symbiolongicarpus studied here. Chapter II describes the isolation of a 300.8 kb alr1-containing chromosomal interval by positional cloning. The analysis of that interval for its gene content and the determination of a primary alr1 candidate, CDS4, are described in Chapter III. Chapter III also reveals the existence of a complex of IgSF-like genes, to which belongs CDS4. CDS4, a novel polymorphic IgSF receptor that encodes a type I transmembrane protein with two hypervariable immunoglobulin-like extracellular domains, was confirmed to be the alr1 allodeterminant in Chapter IV, based on the investigation of natural polymorphism. CDS4 allele sequences were found to largely predict the outcome of allorecognition responses within and between laboratory lines and wild-type colonies, confirming the identity of CDS4 as the classically defined locus alr1.

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