Collagenase Sensitivity and Aggregation Properties of Electrophorus Acetylcholinesterase

Abstract

Tailed forms of Electrophorus acetylcholinesterase, mainly A (9 S) and C (14.2 S) forms, were subjected to [Clostridium histolyticum] collagenase treatment. Several steps were identified, yielding molecules which have lost different portions of the tail and eventually resulting in separation of the isolated tetramers. These modifications result in the disappearance of the low-ionic-strength aggregating properties. The molecules which have retained relatively large fragments of the tail do not aggregate in the same conditions as the intact forms, but still form small aggregates in the presence of high levels of polyanions. A model of the tailed molecules, illustrating the existence of discrete collagenase-sensitive regions in the tail, is discussed.