Human Lymphocyte Membrane (HL-A) Alloantigens: Isolation, Purification and Properties

Open Access
Publisher Website
Google Scholar
Abstract
Human lymphocyte (HL-A) alloantigens have been isolated from human spleen and tissue culture cell sources. Solubilization was accomplished by digesting membrane extracts with papain. About 20% of all the alloantigens detected on the cell membrane were recovered in soluble form. Purification of these materials was achieved by Sephadex chromatography and acrylamide gel electrophoresis. The final purified fraction contained similar levels of several alloantigen specificities. These materials lost alloantigenic activity at low pH, low NaCl concentration, and high temperatures. Comparison of the amino acid composition of alloantigen preparations from two cell sources with different HL-A specificities revealed a general similarity in amino acid content. These proteins contained sialic acid and neutral sugars, but amino sugars were absent. The analytic and quantitative findings indicate that the HL-A alloantigen-carrying molecules have a similar fundamental structure.

This publication has 0 references indexed in Scilit: