ABSTRACT
On the basis of carbohydrate structure, normal dog serum contains three basic types of serum alkaline phosphatase (SAP) corresponding to (1) highly branched complex (non-concanavalin A-binding), (2) complex, or (3) high-mannose (both concanavalin A-binding) oligosaccharide structures. Subsequent binding experiments with monoclonal antibody to intestinal alkaline phosphatase (AP) and bromotetramisole inhibition studies clearly indicated the presence of intestinal-like SAP. Concanavalin A (Con-A) binding characteristics suggested the presence of a bone-like SAP. Con-A-binding and isoelectric focusing results revealed the presence of two (type Ib and IIb) major SAP isoenzymes thought to be of hepatic origin. SAP isoenzymes appear to be modified when compared to tissue AP, particularly in regard to molecular size and, in some cases, carbohydrate structure.
