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Inactivation of factor XIa by plasma protease inhibitors: predominant role of alpha 1-protease inhibitor and protective effect of high molecular weight kininogen.
- C. F. Scott, M. Schapira, H. James, A. Cohen, R. Colman
- BiologyThe Journal of clinical investigation
- 1 April 1982
It is confirmed that alpha(1)-protease inhibitor is the major inhibitor of Factor XIa in plasma, and that the formation of a reversible complex between Factor XI a and HMW kininogen decreases the rate of inactivation of the enzyme by its inhibitors.
Neutrophil elastase-releasing factors in bronchoalveolar lavage from patients with adult respiratory distress syndrome.
- S. Idell, U. Kucich, A. Cohen
- Medicine, BiologyThe American review of respiratory disease
- 1 November 1985
Kallikrein-like activity in the BAL from the patients with ARDS was significantly correlated with the number of neutrophils in the Bal, the neutrophil elastase concentration, and the ability of the BAL to releaseElastase from cytochalasin-B-treated neutrophILS, and there was no correlation between these variables and C5a concentration.
Human plasma kallikrein releases neutrophil elastase during blood coagulation.
- Y. Wachtfogel, U. Kucich, R. Colman
- Biology, MedicineThe Journal of clinical investigation
- 1 November 1983
A series of experiments were carried out to determine if kallikrein was a major enzyme involved in neutrophil elastase release during blood coagulation, and suggest that kallIKrein may be a major enzymes responsible for the release of elastases during bloodCoagulation.
The generation of superoxide anions in glycation reactions with sugars, osones, and 3-deoxyosones.
- B. Ortwerth, H. James, G. Simpson, M. Linetsky
- Biology, ChemistryBiochemical and biophysical research…
- 7 April 1998
Amadori compounds composed of lysine and short chain sugars can rapidly generate superoxide anion in the absence of metal ions.
High molecular weight derivatives of human fibrinogen produced by plasmin. 3. Their NH2-terminal amino acids and comparison with the "NH2-terminal disulfide knot".
- V. Marder, A. Budzynski, H. James
- Biology, ChemistryThe Journal of biological chemistry
- 10 August 1972
A derivative form by proteolytic degradation of fibrinogen, Fragment E, has been shown to be virtually identical with a derivative formed by chemical degradation, the NH2-terminal disulfide knot.
Comparison of three tracers for detecting lung epithelial injury in anesthetized sheep.
- B. Peterson, K. D. Dickerson, H. James, E. Miller, J. McLarty, David B. Holiday
- Biology, MedicineJournal of applied physiology
- 1 May 1989
It is concluded that 99mTc-ALB is the best indicator for studying the effects of lung epithelial injury on protein and fluid transport into and out of the air spaces of the lungs in a minimally invasive manner.
Molecular defect in coagulation factor XFriuli results from a substitution of serine for proline at position 343.
A point mutation that results in coding for serine (TCC) in place of proline (CCC) at amino acid position 343 is found and explains the previous observations of discrete biochemical and functional differences between factor XFriuli and normal factor X.
Spontaneous generation of superoxide anion by human lens proteins and by calf lens proteins ascorbylated in vitro.
The spontaneous generation of superoxide anion in vivo could account for a major portion of the oxidation of sulfur amino acids seen during aging and cataract formation.
Lens proteins block the copper-mediated formation of reactive oxygen species during glycation reactions in vitro.
The data argue that Cu(2+) in the lens would be tightly bound to protein, preventing ROS-mediated AGE formation from glucose in vivo, and increasing levels of Cu( 2+) accelerated the formation of superoxide anion with glucose and fructosyl-lysine.