Calcium-activated neutral protease inhibitor from rabbit erythrocytes lacks the N-terminal region of the liver inhibitor but retains three inhibitory units.
Endogenous inhibitors for calcium-activated neutral protease (CANP) were purified from rabbit erythrocytes and liver. The purified inhibitors showed single bands but with significantly different mobilities on sodium dodecylsulfate-polyacrylamide gel electrophoresis. Peptide mapping and sequencing analyses have revealed that the erythrocyte inhibitor (429 residues) retains the C-terminal three repetitive units of the liver inhibitor (639 residues), which contains four potential repetitive units for inhibition of CANP. The erythrocyte and liver inhibitors inhibited 3 and 4 moles of CANP on the basis of the molecular weights of 46,000 and 68,000, respectively.
D000595:Amino Acid Sequence; D000818:Animals; D002154:Calpain / Q000097:blood*; D002364:Caseins / Q000378:metabolism; D004912:Erythrocytes / Q000032:analysis*; D008099:Liver / Q000032:analysis*; D008970:Molecular Weight; D010449:Peptide Mapping; D011817:Rabbits; D013329:Structure-Activity Relationship
D002364:Caseins; D002154:Calpain