Influence of the Maize Dwarf Mosaic Virns and Simazine upon the Buffer Soluble Proteins and Catalase Activity of a Virus-susceptible and a Virus-tolerant Variety of Zea mays

Inbred corn varieties differing in their tolerance to the maize dwarf mosaic virus infection also differ in varietal character and host response to simazine. Oh 7B, a tolerant cv., has less total soluble and globulin proteins than the sensitive variety, H 55, but more Kjeldahl nitrogen, albumin protein and a doubling of catalase activity. Virus inoculation in Oh 7B causes a reduction in all three protein fractions, Kjeldahl nitrogen and catalase activity. Deleterious virus-simazine interaction does not occur with either variety and the observed varietal and host response differences in protein may account for the conflicting reports of other workers.     

Hemagglutinating Property of Haemophilus aegyptius

Extracts possessing the capacity to hemagglutinate normal human erythrocytes were recovered from Haemophilus aegyptius by treatment with either diethylene glycol or acetone. Antisera prepared against these extracts or the unextracted bacterial cell inhibited hemagglutination by homologous and heterologous antigens. Microgel diffusions indicated the presence of identical components in each extract as expressed by lines of identity between antisera to each fraction. The hemagglutinin was identified as a lipopolysaccharide, 42% lipid and 57% carbohydrate. The determination of 6% phosphorus in the lipid fraction identified it as containing phospholipid.     

Psychological Sequelae of Accidental Injury: A Medico-Legal Quagmire

Litigation for personal injury following accidental trauma is an expensive and confused process involving three protagonists: patient, doctor and lawyer. Although post-traumatic conditions can be elaborately classified, the intrinsic validity of such classifications is often questionable. Current methods of evaluating psychological sequelae of accidental injury are inaccurate and unsatisfactory, partly because of the protagonists'' conceptual, motivational and semantic differences. In addition, there is no really satisfactory method of (a) determining and quantifying minor but significant degrees of brain damage, (b) distinguishing these from “post-traumatic neurosis”, or (c) determining the relationship between the trauma and subsequent disturbance of function. Increasingly “expert” advice is solicited but owing to the nature of the data and conditions of examination, such advice does little to clarify the underlying problems. Furthermore, doctors are often unable to communicate effectively to the judiciary just how the trauma has affected the patient. Even though certain suggestions for improvement are advanced, the need for comprehensive, longitudinal research is inescapable.     

Estimation of secretory rates of hormones from the specific activities of metabolites which have multiple secreted precursors

The calculation of rates of entry of material into an open system of multiple pools in the steady state from the specific activities of end products, which may be derived from several pools, is described. This analysis may be applied to estimate the rates of secretion of steroid hormones from the specific activities of urinary metabolites which may have various hormones as common precursors. In a previous publication (Gurpideet al., 1963) formulae have been presented by which secretory rates could be calculated after a single injection of the tracers assuming that each of the urinary metabolites was uniquely derived from one of the pools in the system. In the present article similar formulae were derived without this assumption. Consequently, it is shown that, under certain circumstances, non-uniquely derived metabolites can be used to estimate secretory rates, and that it may be unnecessary to consider the pathways of conversion of the hormones to the metabolites or the sites where these conversion occur.     

Multiple active forms of thrombin. IV. Relative activities of meizothrombins

The prothrombin activation intermediates meizothrombin and meizothrombin(desF1) (meizothrombin that has been autoproteolyzed to remove fragment 1) have been obtained in a relatively pure, active form with minimal autolysis, making them suitable for enzymatic characterization. When compared at equimolar concentrations, alpha-thrombin, fragment 1.2+ alpha-thrombin, meizothrombin(desF1), and meizothrombin have approximately 100, 100, 10, and 1% activity, respectively, toward the macromolecular substrates factor V, fibrinogen, and platelets. The difference in activity of these four enzymes cannot be attributed to alterations in the catalytic triad, as all four enzymes have nearly identical catalytic efficiency toward the chromogenic substrate S2238. Further, the ability of meizothrombin and meizothrombin(desF1) to activate protein C was 75% of the activity exhibited by alpha-thrombin or fragment 1.2+ alpha-thrombin. All four enzymes bind to thrombomodulin, as judged by the enhanced rate of protein C activation upon preincubation of the enzymes with thrombomodulin. The extent of rate enhancement varied, with meizothrombin/thrombomodulin exhibiting only 50% of the alpha-thrombin/thrombomodulin rate. This difference in rate is not due to a decreased affinity of the meizothrombin for thrombomodulin since the apparent dissociation constants for the alpha-thrombin-thrombomodulin complex and the meizothrombin-thrombomodulin complex are virtually identical. The difference in the observed rate is due in part to the higher Km for protein C exhibited by the meizothrombin-thrombomodulin complex. Incubation of the thrombomodulin-enzyme complex with phospholipid vesicles caused an increase in the protein C activation rates. The kinetic constants for protein C activation in the presence of phospholipid are virtually identical for these enzyme-thrombomodulin complexes. These results suggest meizothrombin generation is targeted toward anticoagulant function such as protein C activation, whereas alpha-thrombin generation is targeted toward procoagulant functions, such as fibrinogen clotting, factor V activation, and platelet aggregation.