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Full-Text Articles in Biochemistry, Biophysics, and Structural Biology

Identification And Analysis Of A Conserved Immunoglobulin E-Binding Epitope In Soybean G1a And G2a And Peanut Ara H 3 Glycinins, Ping Ziang, Tom A. Beardslee, Michael G. Zeece, John P. Markwell, Gautam Sarath Jan 2002

Identification And Analysis Of A Conserved Immunoglobulin E-Binding Epitope In Soybean G1a And G2a And Peanut Ara H 3 Glycinins, Ping Ziang, Tom A. Beardslee, Michael G. Zeece, John P. Markwell, Gautam Sarath

Gautam Sarath Publications

To identify conserved immunoglobulin E (IgE)-binding epitopes among legume glycinins, we utilized recombinant soybean G2a and G2a-derived polypeptide fragments.


Purification And Characterization Of Acylation Stimulating Protein From Porcine Serum, Hong Zhang, Sheila K. Jacobi, Candace F. Toombs, Katherine H. Cianflone, Natalya Nersesian, Gautam Sarath, Jess L. Miner Jan 2002

Purification And Characterization Of Acylation Stimulating Protein From Porcine Serum, Hong Zhang, Sheila K. Jacobi, Candace F. Toombs, Katherine H. Cianflone, Natalya Nersesian, Gautam Sarath, Jess L. Miner

Gautam Sarath Publications

A method for purifying acylation stimulating protein (ASP) from porcine serum is described. The mRNA encoding ASP was cloned by reverse transcriptase-polymerase chain reaction which predicted a 76 residue peptide. Based on this sequence, we generated antisera to a C-terminal peptide (ASP1–20) which aided ASP purification. Identity of the purified protein was verified by N-terminal sequencing. The molecular mass of porcine ASP is 8926. Porcine ASP stimulated esterification of fatty acid into triacylglycerol in cultured human cells with potency similar to that of human ASP (twofold at 5 μM). Based on this evidence that ASP exists in porcine ...