Abstract
A protein with a molecular mass of 85 kDa and an N-terminal sequence resembling polymeric immunoglobulin receptor has been isolated from bovine milk. The isolation procedure involved removal of globulin from acid whey by precipitation with 1.8 M (NH 4) 2SO 4 followed by addition of (NH 4) 2SO 4 to attain a concentration of 3.6 M. Subsequent steps included chromatography on CM-Sepharose and Mono S and elution of the protein of interest with a linear NaCl concentration gradient. The polymeric immunoglobulin receptor-like milk protein inhibited HIV-1 reverse transcriptase (RT) with an IC 50 of 4.8 μM. However, it did not exhibit ribonuclease activity. Neither did it inhibit translation in a cell-free rabbit reticulocyte lysate system.
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