Purification and partial sequence analysis of human T-cell growth factor.

Abstract

A murine monoclonal antibody directed against human T cell growth factor (TCGF) from the JURKAT cell line was used for affinity column purification of the factor. Bound TCGF was eluted nearly quantitatively at low pH, and the recovered factor appeared homogeneous by 2-dimensional gel electrophoresis. The molecule is markedly hydrophobic, with a high content of leucine. A single NH2-terminal sequence of 36 residues was obtained by automated Edman degradation, further supporting the homogeneity of the material. Significant quantities of purified TCGF were prepared in a single step, making possible detailed analysis of its molecular structure and biological role.