PubMed HealthSearch

Biomedical subjects

A Lippin

Publications and source records attributed to A Lippin.

5 recordsLinked to original sources

Inactivation of lipid-enveloped viruses in labile blood derivatives by unsaturated fatty acids.

Virus sterilization of blood plasma derivatives by addition of several naturally occurring fatty acids was evaluated using vesicular stomatitis virus and Sindbis virus as markers for lipid-enveloped virus inactivation and human immunodeficiency virus (HIV). Inactivation of greater than or equal to 10(4) tissue culture infectious doses (TCID50) of marker viruses added to antihemophilic factor (AHF) concentrates, with 60-100% retention of AHF activity, was achieved with oleic, 11-eicosenoic, linoleic, linolenic, palmitoleic and arachidonic acids. Elaidic, gamma-linolenic, palmitic, and arachidic acids and another fat-soluble compound previously reported to inactivate virus, butylated hydroxytoluene, were less effective. A long chain mono- but not a di- or triglyceride also displayed virucidal properties. Evaluation of the inactivation of HIV added to an immune globulin solution on exposure to 0.033% sodium oleate for 20 min indicated inactivation of greater than or equal to 10(3.4) TCID50. The degree of virus inactivation depended on the sample composition. A favorable balance was achieved between degree of virus inactivation and retention of protein function for AHF concentrate, prothrombin complex concentrate, antithrombin III concentrate, and immune globulin solution on incubation with 0.033% (w/v) sodium oleate at 24 degrees C for 4-6 h. Virus inactivation in whole plasma and plasma cryoprecipitate was not complete despite use of higher concentrations of sodium oleate and/or incubation at 37 degrees C. Reduced virus kill in these less purified derivatives probably is a consequence of their endogenous lipid and/or albumin.

Antiviral Agents

Development of hemagglutination assays II. Enhancement in the sensitivity of an RPHA test for HBsAg.

Studies were undertaken to enhance the sensitivity of a previously developed RPHA test for HBsAg. A net increase in sensitivity of approximately 3-fold was achieved by modifying the elution procedure used to purify chimpanzee anti-HBs by affinity chromatography. A further 3- or 4-fold sensitivity increase was achieved by increasing the volume of specimen tested. A concomitant increase in nonspecific agglutination usually observed with increased specimen size was avoided by incubating the reaction mixture at 37 or 45 degrees C. Evaluation of the test in detection of HBsAg in blood obtained from volunteer donors indicates that the materials produced at the New York Blood Center using the modified test protocol compare favorably with a commercial RPHA test. Modifications which did not contribute toward enhancing sensitivity are also reported.

Hemagglutination Tests

Thyroxine binding by hepatitis B surface antigen.

Thyroxine and triiodothyronine binding sites are present on the 20-nm spherical particles associated with hepatitis B surface antigen (HBsAg). Thyroxine-treated HBsAg has a buoyant density of 1.26 g/cm-3 in CsCl and appears under the electron microscope as a hexagonal particle with a center-to-vertex distance of 10 nm. These results provoke questions concerning the origin of thyroid hormone binding sites on HBsAg and a possible relationship between thyroid status and HBsAg antigenemia in humans.

Binding Sites, Antibody

A new reversed passive hemagglutination test for detection of HBsAg.

A new reversed passive hemagglutination test for HBsAg, termed Raphadex B, has been developed using immunochemically purified chimpanzee anti-HBs bound to stabilized human erythrocytes. The test has been found to have equivalent sensitivity to the Ausria 125I radioimmunoassay, and detected a similar number of HBsAg-containing specimens in screening of volunteer blood donors. This method offers an economical approach to third generation methodology for hepatitis B screening of blood donors.

ABO Blood-Group System