Theodore A.W. Koerner

Determinants of red cell, platelet, plasma, and cryoprecipitate transfusions during coronary artery bypass graft surgery: the Collaborative Hospital Transfusion Study

BACKGROUND: Very little is known about the determinants of blood transfusions in patients undergoing coronary artery bypass graft surgery. STUDY DESIGN AND METHODS: To identify factors that influenced the transfusion of red cells, platelets, plasma, and cryoprecipitate, statistical methods were used to study 2476 consecutive diagnosis‐ related group 106 and 107 patients in five teaching hospitals who underwent coronary artery bypass surgery between January 1, 1992, and June 30, 1993. RESULTS: The likelihood of red cell transfusion was significantly associated with 10 preoperative factors: 1) admission hematocrit, 2) the patients age, 3) the patients gender, 4) previous coronary artery bypass surgery, 5) active tobacco use, 6) catheterization during the same admission, 7) coagulation defects, 8) insulin‐dependent diabetes with renal or circulatory manifestations, 9) first treatment of new episode of transmural myocardial infarction, and 10) severe clinical complications. Platelet and/or plasma transfusions were strongly associated with the dose of red cells transfused. Transfusion requirements and other in‐hospital outcomes were associated with patient characteristics, surgical procedure (reoperation vs. primary procedure), and the conduits used for revascularization (venous graft only, venous and internal mammary artery graft, or internal mammary artery graft only). Blood resource use and donor exposures were evaluated with respect to the risk to patients of contracting hepatitis C virus and human immunodeficiency virus infections. CONCLUSION: The classification of coronary artery bypass graft patients on the basis of attributes known preoperatively and by conduits used yields subsets of patients with distinctly different transfusion requirements and in‐ hospital outcomes.

Structure of an extracellular polysaccharide produced by Erwinia chrysanthemi

Erwinia chrysanthemi pv zeae strain SR260, a phytopathogen of corn, produced from lactose an acidic extracellular polysaccharide which was purified and found to consist of L-rhamnose, D-mannose, D-glucose, and D-glucuronic acid in the ratio of 3:1:1:1. A combination of chemical (carboxyl-group reduction, methylation analysis, periodate oxidation, Smith degradation, and lithium-ethylenediamine degradation) and physical (1 and 2D NMR spectroscopy) methods revealed that the polysaccharide is composed of a hexasaccharide repeating unit 1: [formula: see text]

Human platelets express gangliosides with LKE activity and ABH blood group activity.

BACKGROUND: Platelets express several neutral glycosphingolipids with ABH and P blood group activity that may play a role in infectious, autoimmune, and alloimmune thrombocytopenia. In RBCs, sialylated glycosphingolipids or gangliosides with blood group activity have also been reported. To determine whether similar antigens are expressed by platelets, the total platelet ganglioside fraction was isolated and screened for blood‐group‐active glycosphingolipids.

Extracellular polysaccharide of Erwinia chrysanthemi

Abstract The extracellular polysaccharide (EPS) produced by E. chrysanthemi pv. zeae strain SR260, a strain pathogenic to corn, has a branched hexasaccharide repeat unit consisting of a glucomannorhamnan backbone [ → 3)-β- d - Glc p-(1 → 4)-α- d - Man p-(1 → 3)-α- l - Rha p-(1 → ] and a trisaccharide side-chain [ α- l - Rha p-(1 → 3)-α- l - Rha p-(1 → 4)?- GlcA p-(1 → ] attached to O-3 of the mannose in the backbone [1]. All the anomeric configurations, except that of the rhamnosyl-glucosyluronic linkage in the side chain, were unambiguously assigned by a combination of 1 and 2D NMR spectroscopy. The tentative assignment of the rhamnosyl-glucosyluronic glycosyl linkage as α- l is now proven.

Evidence of a Phospholipid Binding Species within Human Fibrinogen Preparations

Fibrinogen has been reported to interact with phospholipid; however, the properties of this binding interaction have not been characterized. Purified preparations of human fibrinogen bound to small unilamellar vesicles containing phosphatidylserine (PS) as measured by light scattering and radioisotope filtration. Binding to 100% PS was saturable (apparent Kd=5 microM, Bmax=1.9 g protein/g lipid), reversible, and involved a minor subfraction of the fibrinogen preparation (3-6% of total protein). Fibrinogen interacted minimally with phosphatidylinositol, and not at all with pure phosphatidylcholine (PC) or PC vesicles containing 5% glycosphingolipid (lactosylceramide, ganglioside GM3, ganglioside GD3). Binding efficiency decreased as the PS content of vesicles was diluted with PC. Calcium chloride (2 mM) enhanced protein binding to PS, which was reversed by EDTA. Fibrin clot formation almost quantitatively precipitated the PS binding activity. PS, but not PC, increased the final turbidity of fibrin clots. Computerized sequence analysis of fibrinogen revealed three candidate acidic phospholipid binding motifs located at position 143-210 in the alpha chain, and positions 59-77 and 101-139 in the beta chain. Further study of the PS binding activity of fibrinogen may lead to new insights about fibrinogen function.

A quantitative analysis of H-2 linked effects on hepatic ganglioside composition

We have conducted a quantitative analysis of the gangliosides extracted from brain, spleen, thymus, and liver tissue of 8-week-old male mice from H-2 congenic mouse strains on the B10 background, using high performance thin-layer chromatography (HPTLC). An analysis of variance of replicate samples of liver from strains B10, B10.A, and B10.G revealed that the time of sample and colony of origin were not sources of significant variance but that for N-glycolylated gangliosides GM2, GM1, and GD1a, the differences detected between strains were significant. Particularly important were the differences for GM1: the values of 0.0% for B10, 19.0% for B10. A, and 36.0% for B10.G were each significantly different from the others (P<0.0005). Further studies with liver tissue from B10/A H-2 recombinant strains also revealed three significantly different levels of GD1a: ⩽4.0% [B10, B10.A (3R), B10.A (5R), B10.A (18R)], 11.0% (B10.A), and 33% [B10.A (1R), 1310.A (2R), B10.A (4R)]. Our findings support prior studies which indicate that a gene linked to the H-2 complex affects hepatic GM2 galactosyltransferase activity. However, they also indicate that the current model, which classifies all strains as possessing either an allele for “high” enzyme activity or a single alternative allele for “low” enzyme activity, is probably oversimplified, since at least three levels of enzyme activity appear to exist as stable phenotypic markers. Moreover, the current model cannot readily account for the three different levels of GD1a observed with B 10/A H-2 recombinants. Alternative models are proposed, including the novel suggestion that a distinct H-2 linked gene may affect hepatic GM1 sialyltransferase activity. These findings demonstrate that further study of H-2 linked genes affecting the activities of glycosyltransferases is indicated.

TREHALOSE AS A COMMON INDUSTRIAL FERMENTATION BYPRODUCT

Abstract During the analysis of several industrial fermentation byproduct streams significant amounts of α,α-trehalose and α,β-isomaltose were found. These disaccharides were purified from one of the fermentation-byproduct streams and identified by chromatography and 600-MHz 1 H NMR. Examination of fermentation streams before and after the addition of active organisms established that α,α-trehalose is a product of the fermentation and α,β-isomaltose is a component of the starting nutrients. Analysis of a number of agribusiness industrial-byproduct streams has had the objective of identifying compounds of potential value for isolation, or determing those that may be toxic to microorganisms in the anaerobic methanogenesis of organic compounds in the streams. The frequent occurrence of two disaccharides was noted in those streams from fermentation processes and prompted this study.

Two-dimensional 1H-, 13C-, and 31P-nuclear magnetic resonance and molecular-mechanics investigation of d-fructose 2,6-bisphosphate

Two-dimensional nuclear magnetic resonance studies have been carried out to assign unequivocally all the proton, carbon, and phosphorus resonances of D-fructofuranose 2,6-bisphosphate (1) and to verify its structure using a 400-MHz spectrometer. Several unexpected chemical-shift values and coupling constants were obtained. Molecular mechanics calculations (Sybyl) carried out to minimize the conformational energy of 1 yield phi C-1,P-2 = + 84, phi C-3,P-2 = - 155, and phi C-5,P-6 = + 175. Thus the unusual near-gauche orientations of C-1 and C-3 to P-2 in 1 can explain their small vicinal coupling constants (3JC-1,P-2 = 1.2, and 3JC-3,P-2 = 3.8 Hz), in contrast to the expected larger value seen for 3JC-5,P-6 namely, 6.9 Hz. Treatment of a sample of this compound with sodium borohydride did not affect its nuclear magnetic resonance spectrum, substantiating that O-2 is phosphorylated. Oxidation with sodium periodate yielded an intermediate which decomposed by a beta-elimination mechanism involving the 6-phosphate group. These data establish unequivocally the 1H, 13C, and 31P assignments and explain the observed anomalous shifts. Moreover they indicate that the activator of fructose 6-phosphate 1-kinase is the beta anomer of the 4T3 conformer of D-fructose 2,6-bisphosphate.