Efficiency of Radiolabeling Eggs Before and After Microwave Cooking for Gastric Emptying Scintigraphy Studies.

The accuracy and reproducibility of nuclear medicine gastric emptying scintigraphy (GES) require strict adherence to the Society of Nuclear Medicine and Molecular Imaging standardized protocol, which contains precise instructions for meal ingredients and preparation. Previous research demonstrated that many laboratories were using whole eggs in the test meal as opposed to the guideline-recommended liquid egg whites and that some laboratories were attempting to radiolabel the egg by adding the radiotracer after cooking. This study aimed to document the labeling efficiency of Tc-sulfur colloid (SC) added to whole eggs before and after microwave cooking.

An unbiased systems genetics approach to mapping genetic loci modulating susceptibility to severe streptococcal sepsis.

Striking individual differences in severity of group A streptococcal (GAS) sepsis have been noted, even among patients infected with the same bacterial strain. We had provided evidence that HLA class II allelic variation contributes significantly to differences in systemic disease severity by modulating host responses to streptococcal superantigens. Inasmuch as the bacteria produce additional virulence factors that participate in the pathogenesis of this complex disease, we sought to identify additional gene networks modulating GAS sepsis.

Structural features of the ligand binding site on human complement protein C8gamma: a member of the lipocalin family.

Human C8 is one of five components of the cytolytic membrane attack complex of complement. It contains three subunits (C8alpha, C8beta, C8gamma) arranged as a disulfide-linked C8alpha-gamma heterodimer that is noncovalently associated with C8beta. C8gamma has the distinction of being the only lipocalin in the complement system.

Incorporation of human complement C8 into the membrane attack complex is mediated by a binding site located within the C8beta MACPF domain.

Human C8 is one of five complement components (C5b, C6, C7, C8, C9) that interact to form the membrane attack complex (MAC). C8 is an oligomeric protein composed of a disulfide-linked C8alpha-gamma heterodimer and a noncovalently associated C8beta chain. C8alpha and C8beta are homologous; both contain N- and C-terminal modules and an intervening approximately 40 kDa segment referred to as the membrane attack complex/perforin (MACPF) domain.