The effects of atrial polypeptide and neurohormone C upon the interaction of human factor Xa (FXa) and human antithrombin III (ATIII) were followed by sodium dodecyl sulfate polyacrylamide gel electrophoresis. A pattern of bands consisting of a 1 degree duplex complex (FXaalpha-ATIII band of 109 kDa, FXabeta-ATIII band of 104 kDa), a 2 degree duplex complex (alpha band of 99 kDa, beta band of 95 kDa), a 3 degree duplex complex (alpha band of 66 kDa, beta band of 62 kDa), modified ATIII (ATIIIM, 58 kDa), native ATIII (55 kDa), FXaalpha (52 kDa), FXabeta (47 kDa), and a FXa degradation product (FXagamma, 35 kDa) was detected and quantitated. Preincubation of FXa, ATIII, or mixtures thereof with atrial polypeptide produced a shift from FXaalpha-ATIII to FXabeta-ATIII complexes and increases in both ATIIIM and FXagamma, reflecting degradation of the 1 degree and 2 degree complex to form the 3 degree complex.
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