Ching-Tso Wang

Analysis of different forms of recombinant human leukocyte interferons and synthetic fragments by high-performance liquid chromatography

Analytical high-performance liquid chromatography (HPLC) conditions are reported for the evaluation of recombinant human interferon monomers: recombinant human leukocyte interferon A (rIFN-alpha A), rIFN-alpha D, and the hybrid rIFN-alpha A1-62/D64-166. The two monomeric forms of rIFN-alpha A (slow-migrating monomer and fast-migrating monomer) were also resolved by HPLC. Conditions are reported for the HPLC separation of oligomers (dimers and trimers) of rIFN-alpha A. The synthesis and analytical HPLC of the carboxy-terminus fragment, corresponding to IFN-alpha D (140-166), and a series of analogues comprising the IFN-alpha A (105-125) region is reported. The syntheses were accomplished by the solid-phase peptide synthesis procedure and the products were purified by preparative HPLC.

The Synthesis and Physical Properties of Thymosin α1 and Its Analogs Prepared by Fragment Condensation

The isolation of biologically important peptides from the thymus gland has been studied extensively in the last few years. Several thymic peptides have been shown to play certain roles in T-cell maturation (White, 1980; Trainin et al., 1980a, b; Goldstein and Lau, 1980; Bach and Goldstein, 1980). Thymosin α1, a highly acidic Nα-acetyl octacosapeptide, isolated from calf thymus gland (Goldstein et al., 1977) and characterized by sequence analysis (Low and Goldstein, 1979), has been reported to exhibit biological activities involved in the development of thymus-dependent lymphocytes (T cells) (Goldstein et al., 1977). Thymosin a1 has been synthesized by classical procedures in solution (Wang et al., 1979; Birr and Stollenwerk, 1979) and by solid-phase methods (Wong and Merrifield, 1980; Wang et al., 1980; Colombo, 1981).