Evidence of a small hydrophobic domain in the core protein of the heparan sulfate proteoglycan from human colon carcinoma cells

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Abstract
We demonstrate that the cell surface heparan sulfate proteoglycan of human colon carcinoma cells has an affinity for a hydrophobic matrix. This property is mediated by sequences in the core protein, since papain‐or alkaline borohydride‐released heparan sulfate chains do not bind to the matrix. Trypsin releases a [3H]leucine‐rich, unsulfated, hydrophobic peptide, with M r ~ 5000. This domain is present in neither the proteoglycan released into the medium nor in the intracellular degradation products. It is proposed that this peptide may represent the portion of the core protein intercalated into the plasma membrane.