Antibodies to reverse transcriptase in HIV infection and progression to AIDS.

Serum antibodies to the reverse transcriptase (ART) of human immunodeficiency virus 1 (HIV-1) were sequentially determined by ELISA in a group of 41 HIV-seropositive male homosexuals and 101 matched healthy controls, over 1.5-6 years (mean follow-up 3.25 years).

Expression and biochemical characterization of human immunodeficiency virus type 1 nef gene product.

nef genes from human immunodeficiency virus type 1 isolates BH10 and LAV1 (lymphadenopathy-associated virus type 1) were expressed in Escherichia coli under the deo operon promoter. The two proteins found in the soluble compartment of the bacterial lysate were purified by ion-exchange column chromatography to apparent homogeneity. Determination of the amino-terminal sequence revealed glycine as the first amino acid in the Nef protein, indicating removal of the initiator methionine during expression in E.

Pharmacokinetics of recombinant human superoxide dismutase.

Superoxide dismutase (SOD) disposition was studied in order to design a rational approach for drug administration in the setting of acute myocardial infarction. Four chronically instrumented conscious dogs received the following dosage regimens of recombinant human SOD (rhSOD) on successive days: (a) 5 mg/kg left atrial (LA) bolus, (b) 5 mg/kg central vein (CV) bolus, (c) 15 mg/kg CV bolus, and (d) 5 mg/kg CV infusion over 60 min; additionally, all dogs received (e) a 5 mg/kg CV bolus under pentobarbital anesthesia. Serial serum samples were obtained after each dose and serial myocardial samples were obtained after dose (e).

High-level expression of enzymatically active human Cu/Zn superoxide dismutase in Escherichia coli.

Expression of human Cu/Zn superoxide dismutase (SOD) with activity comparable to the human erythrocyte enzyme was achieved in Escherichia coli by using a vector containing a thermoinducible lambda PL promoter and a beta-lactamase-derived ribosomal binding site. The recombinant human SOD was found in the cytosol of disrupted bacteria and represented greater than 10% of the total bacterial protein. The enzyme was purified to homogeneity by salt precipitation, gel filtration chromatography, and ion exchange chromatography.

Tunicamycin blocks neuritogenesis and glucosamine labeling of gangliosides in developing cerebral neuron cultures.

Fetal cerebral neurons at the initiation of active neurite outgrowth in culture incorporate 4-fold more [3H]glucosamine into glycoproteins than into the cellular lipid fraction. After 8 days or longer, when a well-developed fiber network is apparent, lipids are labeled more extensively than the glycoproteins. Labeling of the latter is inhibited 95% and 89% by 0.