On the quaternary structure of leucine aminopeptidase.
Small crystals of leucine aminopeptidase were prepared in 2 percent ammonium molybdate. Single molecules were contrasted with 2 percent potassium silico tungstate which gave better contrast and preservation of enzyme activity than ammonium molybdate. The six subunits of the enzyme consist of a spheroidal "head" and some "tail-like" material, which connects the "heads" in pairs. The subunits are arranged at the vertices of either a right triangular prism or of an oblique prism twisted by 42 degree (symmetry 32).
D000818:Animals; D002417:Cattle; D003459:Crystallins / Q000032:analysis; D003460:Crystallization; D007908:Lens, Crystalline / Q000201:enzymology; D007931:Leucyl Aminopeptidase / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D010316:Particle Size; D013329:Structure-Activity Relationship
D003459:Crystallins; D007931:Leucyl Aminopeptidase