Thrips and Bollworm Control in Bt Cotton 1996

Cotton was planted 25 May 1996 on the Judd Hill Plantation near Truman, AR in Mhoon sandy loam soil. Plots were 8 rows (38 inch centers) wide and 40 ft long separated by 2 unplanted rows and 10 ft alleys. Irrigation was supplied by flooding furrows. Treatments were arranged in a RCBD with 4 replications. Temik was applied at planting using Gandy boxes. The sidedress application was made on 3 Jul. Baythroid was applied using a 4-row CO2 charged backpack sprayer calibrated to deliver 13 gpa at 20 psi with 1 TJ-50 8002vs nozzle per row. Thrips were monitored by using whole plant washes of a detergent mixture with an alcohol rinse. Plants were monitored for pest insects and damage through the season and were mapped at harvest.

Quantification of apolipoprotein A-IV in human plasma by immunonephelometry

We developed a nephelometric procedure for determining concentrations of human plasma apolipoprotein (apo) A-IV. Results obtained correlate well with those measured by an established electroimmunodiffusion assay (r = 0.98; n = 56). Intra- and interassay CVs were 2.4% and 2.0%, respectively, indicating excellent precision and reproducibility. Various conditions of sample treatment, such as adequate storage, freezing, and thawing, did not affect results significantly. However, keeping samples at room temperature for 4 days led to a slight increase in measured values. Preincubation with a cholesterinesterase-detergent mixture abolished interference from triglyceride-rich lipoproteins, allowing assay of samples containing triglycerides as great as 10 g/L. The assay is easily applicable to clinical laboratories for routine diagnostic use, as shown with hypertriglyceridemic plasmas and samples with a broad range of apo A-IV concentrations.

Treatment of Hemophilia A with a Highly Purified Factor VIII Concentrate Prepared by Anti-FVIIIc Immunoaffinity Chromatography

SummaryTo reduce the risk of pathogenic virus transmission associated with the therapeutic administration of plasma-derived antihemophilic factor (FVIIIc), a process utilizing anti-FVIIIc immunoaffinity chromatography to isolate FVIIIc has been developed. In addition, the starting cryoprecipitate solution has been treated with an organic solvent/detergent mixture to inactivate lipid-enveloped viruses. A final ion exchange chromatography step is used to further remove contaminants, e.g., anti-FVIIIc antibody, potentially leached with FVIIIc during the immunoaffinity step. The purified FVTII is stabilized for lyophili-zation and storage by the addition of human albumin. The monoclonal anti-FVIIIc antibody used in the immunoaffinity step of the process is not detectable in the final preparation. Viral reduction studies performed at specific steps of the process demonstrate that 11 logs of human immunodeficiency virus (HIV) and greater than 4-5 logs of other lipid-enveloped viruses are inactivated within the first 30 s of exposure to the solvent/ detergent mixture and 4-5 logs of various model viruses, e. g. Endomyocarditis virus (EMC), are physically removed during washing of the immunoaffinity column. The lyophilized product is reconstituted using sterile water in a matter of seconds.The pharmacokinetics of Hemofil® M were compared to those obtained using a standard heat-treated concentrate (Hemofil® CT) in five severe factor VIII deficient hemophiliacs in a randomized, cross-over study. No statistically significant differences were observed in mean half life (p >0.6) or median recovery (p = 0.4) between the two preparations. No clinically significant adverse effects were observed in patients receiving either FVIII preparation.In addition, 43 patients at 18 different centers underwent pharmacokinetic studies, with a nominal dose of 50 u/kg FVIIIc Hemofil® M. The mean recovery was 103.6%, and the t 1/2 was 14.6 h. The recovery of FVIII in this group was as expected, providing an increase of assayed FVIII of approximately 2% per unit of FVTII/kg infused.Clinical trials using Hemofil® M have been initiated in 124 hemophilia A patients. The safety and efficacy of Hemofil® M has been established. To date, 0 of 60 patients tested have seroconverted to HIV. None of the previously untreated patients show clinical or laboratory evidence of Non-A, Non-B hepatitis (NANB), with 21 patients remaining negative as far as presence of antibodies to the Hepatitis C virus (a-HCV negative) at least 6 months after the initial infusion. There is no evidence of neoantigenicity, evidenced by seroconversion to murine antibody. An 8.7% (2 of 23) prevalence of anti-FVIIIc inhibitor development has been observed in previously untreated patients with FVIIIc⩽3%, receiving only the monoclonally purified solvent/ detergent treated FVIII concentrate while on study and on poststudy surveillance. All patients demonstrated clinical hemostasis following product use for either on demand bleeding or surgical prophylaxis.

PREPARATION OF HIGH SPECIFIC ACTIVITY PLASMA AHF BY ANTI-FVIIIc IMMUNOAFFINITY CHROMATOGRAPHY

To reduce the risk of pathogenic virus transmission associated with the therapeutic administration of plasma derived AHF (FVIIIc) we have developed a process wherein anti-FVIIIc immunoaffinity chromatography is used to isolate FVIIIc from a cryoprecipitate solution which has been treated with an organic solvent/detergent mixture to inactivate 1-ipid-enveloped viruses. A final ion exchange chromatography step is used to further remove contaminants (eg. anti-FVIIIc antibody) eluted with FVIIIc during the immunoaffinity step. FVIIIc obtained in the process has a specific activity of 1500 to 2000 AHF units (one stage clotting assay) per mg of protein, representing a ≥120,000-fold purification from plasma. The purified FVIIIc is stabilized for lyophilization and storage by the addition of human albumin. Polyclonal anti-FVIIIc immunoblots reveal polypeptides with apparent mol wts between 90,000 and 230,000 (heavy chain) and 70,000 to 76,000 (light chain). The major လcontaminant” in the preparation is von Willebrand Factor, one mol (Mr = 250,000 subunit) per mol of FVIIIc. Fibrinogen and fibronectin are barely detectable in the final preparation at levels of 1.0 and 0.3 ng per AHF unit respectively, representing a 3 million-fold purification of FVIIIc relative to these proteins. Anti-FVIIIc antibody, used in the immunoaffinity step of the process, is not detectable in the preparation at levels of 2.0 ng/mL (i.e. ≤0.01 ng per AHF unit). The extent to which virus reduction is associated with the process was also evaluated. The addition of an organic solvent/detergent mixture to cryoprecipitate solution resulted in HIV (and other lipid-enveloped viruses) inactivation to levels below the level of assay sensitivity in <5 min; representing a measurable 4 to 5 log reduction in virus titer. In addition, substantial (nonenveloped and lipid-enveloped) virus reduction was associated with the immunoaffinity step used in the process (3,400 to 50,000-fold depending on the virus/experimental conditions studie). The overall process results in a high specific activity AHF preparation which also appears to be substantially improved over previous AHF preparations with respect to viral contamination.

The Upper Cortex of Parmelia Saxatilis and other Lichen Thalli

A method, including treatment with an enzyme/detergent mixture, of revealing features of the cortical hyphal arrangement in lichen thalli is described. The cortex structure of Parmelia saxatilis, Xanthoria parietina, Hypogymnia physodes and Lecanora muralis is illustrated and described.