Proteolytic fragmentation of fibrinogen. I. Comparison of the fragmentation of human and bovine fibrinogen by trypsin or plasmin.
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Biomedical subjects
Publications and source records attributed to R M Weinberg.
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Two boys are presented who fulfilled criteria for a diagnosis of idiopathic pulmonary hemosiderosis. A lung biopsy specimen from the first patient showed alveolar-capillary basement membrane abnormalities, together with abnormalities of capillary endothelial cells and hemosiderin-laden macrophages. A lung biopsy specimen from the second patient showed mainly capillary endothelial abnnormalities and interestitial fibrosis. Both patients had a noticeable improvement in symptoms and relative stabilization of their roentgenographic and pulmonary function abnormalities following azathioprine therapy.
The effect of ipratropium bromide administered at two dosage levels, 40 and 80 mug, isoproterenol, 150 mug, and placebo using a metered dose inhaler was evaluated in ten adult patients with asthma in a double-blind, crossover study. The new atropine-like drug proved to be as effective a bronchodilator as isoproterenol in this study, although it had a later peak effect. Ipratropium bromide had a longer course of action than isoproterenol (4 hours compared to 1-2 hours) and was free of significant side effects. The larger dose of the new drug produced a slightly greater and longer-acting effect than the smaller dose. Ipratropium bromide seems to have had bronchodilator effects on both large and small airways.
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Native bovine factor V exhibits a molecular weight of 300000 as determined by gel filtration of untreated plasma. Highly purified factor V exhibits multiple molecular weight forms which range from small active fragments to aggregates of several million which are generated during the purification on cellulose phosphate. Isoelectric focusing on a single high-molecular-weight species produced a single protein and activity peak at pH 4.65. Factor V activity is associated with each protein band observed following polyacrylamide gel electrophoresis. Antisera to factor V prepared in rabbits produces a time-dependent and concentration-dependent inhibition of factor V activity in plasma and purified factor V. The multiple molecular weight forms of factor V appear equivalent upon immunodiffusion and on immunoelectrophoresis migrate as an alpha globulin between albumin and fibrinogen. Immunoprecipitation arcs are equivalent in plasma and serum. Factor V consists of two major types of subunits, a light chain (73000), aggregates of which form the high-molecular-weight species, and a heavy chain (125 000). Using preparations containing one or both chains isolated by disc gel electrophoresis, antiserum was shown to contain two families of antibodies, one against each subunit. Cross reactivity with both light and heavy chain antigens is observed in sheep and goat but not monkey or human plasma. The antisera also neutralized goat and sheep factor V activity.