American Society of Hematology

Fig. 1.

$Fig. 1. Binding of fractionated eluted leukemia-associated peptides to HLA-A2 and -B7 molecules. (A) Acid-eluted peptides were fractionated by HPLC and detected by absorbance at 214 nm. (B) Individual fractions were assayed for their ability to promote HLA-A2 and -B7 assembly. The influenza virus matrix peptide, M58-66, and an endogenous peptide, (APRTVALTAL), are HLA-A2 and -B7 ligands and were used as positive controls (T). The values obtained with the negative control peptide NP 383-391 (nonspecific binding) have been substracted from the results shown. Means of duplicates and standard deviations are given.$

Binding of fractionated eluted leukemia-associated peptides to HLA-A2 and -B7 molecules. (A) Acid-eluted peptides were fractionated by HPLC and detected by absorbance at 214 nm. (B) Individual fractions were assayed for their ability to promote HLA-A2 and -B7 assembly. The influenza virus matrix peptide, M58-66, and an endogenous peptide, (APRTVALTAL), are HLA-A2 and -B7 ligands and were used as positive controls (T). The values obtained with the negative control peptide NP 383-391 (nonspecific binding) have been substracted from the results shown. Means of duplicates and standard deviations are given.

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