Amyloid beta (A beta) is a normal proteolytic fragment of a large precursor protein (beta PP) which undergoes altered conformation, leading to fibril formation. Two main beta PP processing pathways have been described, and we are now reporting the characterization of a third beta PP pathway. A membrane-associated 16 kDa component identified in human platelets isolated from normal donors. Based on size, immunoreactivity and amino acid sequence analysis, the fragment is a C-terminal beta PP component which starts at position 642 (APP770 numbering) and contains the intact A beta sequence. The presence of this novel pathway of beta PP processing in resting platelets suggest that it occurs as a normal event.