Orientation of the NADPH dependent superoxide generating oxidoreductase on the outer membrane of human PMN's.
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Biomedical subjects
Publications and source records attributed to T R Green.
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Proteinase inhibitor II, an inhibitor of chymotrypsin and trypsin, is a heat-stable protein with a dimeric molecular weight of 21 000 that is a component of Russet Burbank potato tubers. Four monomeric isoinhibitor species of molecular weight 10 500 comprise inhibitor II and were isolated by chromatography on phosphocellulose in 8 M urea. Upon removal of the urea, each monomeric species dimerized to yield homogeneous dimers. The three major protomer species, called B, C, and D, and their homogeneous dimers were further characterized. They have similar molecular weights and amino acid compositions, and each has an N-terminal alanine residue. Dimers of purified protomers B, C, and D exhibited full cross-reactivities with each other in immunological double-diffusion assays. Reconstituted dimers possess two binding sites for bovine alpha-chymotrypsin, indicating that each monomer possesses one binding site for this enzyme. Significant differences were noted among the reconstituted dimers in their isoelectric points, immunoelectrophoretic mobilities, ion-exchange properties, and their inhibitory reactivities against trypsin. The properties of the inhibitor II dimeric species are similar but not identical to inhibitors IIa and IIb reported from Japanese potatoes (variety "Danshaku-Imo"), indicating the existence of intervarietal, as well as intravarietal, differences among potato tuber inhibitor II isoinhibitors.
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Wounding of single leaflets of young tomato (Lycopersicum esculentum var. Bonnie Best) plants causes the release of a proteinase inhibitor inducing factor. This factor is rapidly transported throughout the plant where it causes accumulation of inhibitor I, a potent inhibitor of several serine proteinases from both animals and microorganisms. The wound-induced accumulation of inhibitor I is both light- and temperature-dependent. In total darkness no accumulation results from wounding. The accumulation exhibits a linear dependence upon light up to 300 foot candles. At 600 foot candles and above, the response is maximal. In light the wound response possesses an unusual temperature dependence with an optimum rate of accumulation near 36 C. Below 20 C no accumulation occurs. The over-all process contains two light- and temperature-dependent steps, one involving wounding and transport, the other involving accumulation.
The activities of individual enzymes of the isoprenoid pathway from mevalonate kinase to squalene synthetase in homogenates of seeds germinated up to 32h were assayed. Changes in the activity of each enzyme were observed and compared with the activity at the 2h germination stage. Activities of alkaline phosphatase and fructose 1,6-diphosphate aldolase were similarly measured to provide a reference for changes in the general metabolic activity of seeds during imbibition of water. Water uptake reached a plateau after 12h. The reference enzymes almost doubled in activity between 2 and 8h and thereafter their activities steadily declined. All of the enzymes of the isoprenoid pathway increased in activity between 2 and 6h and, thereafter, with the exception of the prenyltransferase, their activities remained relatively constant. With the prenyltransferase activity the initial increase was followed by a short plateau between 6 and 9h and then a second increase to a maximum between 14 and 16h. After 16h the activity declined. The relative activities of the isoprenoid enzymes at 16h of germination were mevalonate kinase>phosphomevalonate kinase>pyrophosphomevalonate decarboxylase approximately isopentenyl pyrophosphate isomerase>squalene synthetase>isopentenyl pyrophosphate/dimethylallyl pyrophosphate prenyltransferase. The finding that the prenyltransferase may be the rate-limiting enzyme in squalene synthesis from mevalonate is discussed in relation to regulation of isoprenoid synthesis during pea-seed germination.
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A double substrate immunoassay has been developed that allows simultaneous quantitation and localization of red blood cell surface antigens. The assay can be used to quantitate surface antigens, or the titer of antisera specific to cell-surface antigens, on the red blood cell. The assay has been adapted to the study of both D antigen and erythrocyte membrane (EM) antigen, which were found to be uniformly dispersed over the surface of the cell. The number of EM antigens per cell appeared to be approximately twenty times that of the D antigen. For typing antisera, this assay makes it feasible to express antibodies in absolute units (microgram antibody) rather than conventional dilution titers, and thus offers a simpler means of rapidly comparing antisera.
OBJECTIVE: To demonstrate that creatine kinase-MB fraction (CK-MB) elevations within three hours of presentation in the emergency department (ED) are associated with subsequent ischemic events in clinically stable chest pain patients. METHODS: Prospective cohort study at two university- affiliated teaching hospitals. Participants were consenting ED chest pain patients 25 years old or older without evidence of rhythm or hemodynamic instability (n = 449). Exclusions included ST-segment elevation > or = 0.1 mV in > or = 2 electrocardiogram leads, chest wall trauma, abnormal x-ray studies, and incomplete data collection. Measurements included presenting and three-hour CK-MB levels, presenting ECG, initial clinical impression of coronary care unit need, and clinical follow up. Monitored adverse events included myocardial ischemia necessitating coronary angioplasty or cardiac bypass surgery, recurrent in-hospital myocardial infarction, bradycardia requiring pacing, emergent cardioversion, cardiogenic shock, ventricular fibrillation, and death. RESULTS: Overall, nine (2%) of 449 patients experienced an ischemic event within the first 48 hours. All nine patients required either coronary angioplasty or bypass surgery. Four (44%) of the nine patients with 48-hour ischemic events had elevated CK-MB levels. Of 23 patients who had complications within one week of ED presentation, seven (30%) had elevated ED CK-MB levels. An elevated CK-MB level was associated with an ischemic event both within 48 hours (risk ratio 9.5; 95% CI 2.7-33.7) and within one week (risk ration 5.2; 95% CI 2.3-11.7). CONCLUSIONS: An elevated CK-MB level within three hours of ED presentation is associated with a subsequent ischemic event in the clinically stable chest pain patient without ST-segment elevation. However, the ED CK-MB identifies only a minority or otherwise low-risk patients who develop ischemic events; other markers for diagnosing myocardial ischemia in the ED are needed.