Effect of Glutamine on Phagocytosis and Bacterial Killing by Normal and Pediatric Burn Patient NeutrophilsCora K. Ogle, James D. Ogle, Ju‐Xian Mao et al.|Journal of Parenteral and Enteral Nutrition|1994 Glutamine is essential for the function of lymphocytes and macrophages, where it serves, among other things, as a source of energy. Little information is available concerning the fuel that polymorphonuclear cells use for their metabolic and bactericidal functions. It was the purpose of this study to determine whether glutamine would enhance the in vitro bactericidal function of normal neutrophils and whether the amino acid would restore the observed impaired function in burn patients to or above the normal level. Twelve burn patients with total body surface area burns ranging from 32% to 87% were studied. At various postburn times, neutrophils were isolated and their ability to kill Staphylococcus aureus in the presence and absence of glutamine was determined and compared with that in normal subjects. Glutamine enhanced the bactericidal function of normal neutrophils. In every patient, at all but two postburn times, glutamine caused an improvement in the observed abnormal neutrophil bactericidal function and often restored it to or slightly above the normal level. Glutamine had no effect on the expression of C3b receptors (CR1 or CD35) or on phagocytosis by the cells. This study confirms the beneficial effects of glutamine in at least one arm of the immune system and adds evidence for the possible advantage of including this amino acid in the diets of burn and other trauma patients.
3-Hydroxyproline, a New Amino Acid of CollagenConsumptive OpsoninopathySerum levels of properdin, Factor B and C3 and the ability of these sera to opsonize E. coli 075 were measured in 17 patients with surgical infections ranging in severity from mild to fatal. There was good direct correlation between severity of infection, serum levels of properdin and C3, and the ability of the serum to support opsonization. The levels of Factor B were not significantly reduced when measured by radial immunodiffusion, but immunoelectrophoresis showed conversion. Restoration of full opsonic activity was accomplished only by the addition of a combination of C3, Factor B, and properdin in excess. The findings provide evidence that severe bacterial infection causes a consumption of opsonic proteins which may result in a reduced ability of the patient's serum to opsonize bacteria and thereby further increase susceptibility to infection.
Properties of an insoluble form of trypsinADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTProperties of an insoluble form of trypsinJames D. Ogle and Cora K. GlassmeyerCite this: Biochemistry 1971, 10, 5, 786–792Publication Date (Print):March 1, 1971Publication History Published online1 May 2002Published inissue 1 March 1971https://pubs.acs.org/doi/10.1021/bi00781a010https://doi.org/10.1021/bi00781a010research-articleACS PublicationsRequest reuse permissionsArticle Views119Altmetric-Citations65LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
Two Tripeptides from an Enzymatic Digest of Collagen