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J. Biochem, 1990, Vol. 108, No. 1 80-85
© 1990 Japanese Biochemical Society


research-article

Amino Acid Sequence at the Reactive Site of Rabbit {alpha}-1-Antiproteinases

Akio Saito and Hyogo Sinohara

Department of Biochemistry, Kinki University, School of Medicine Osaka-Sayama, Osaka 589

Rabbit {alpha}-1-antiproteinases S and F were treated with trypsin, chymotrypsin, Staphylococ-cus aureus protease V8, and thermolysin, and the liberated peptides encompassing the reactive region of the respective inhibitors were separated and sequenced. The reactive center of the F form was methionine, and the residues from P3 to P'1 (Ile-Pro-Met-Ser) were the same as those of human {alpha}-1-antiproteinase. The S form, on the other hand, was found to be a mixture of two distinct proteins (S-1 and S-2), and their reactive centers (P1-P'1) were Ser-Ser and Tyr-Ser, respectively. Seven out of 17 amino acids in the F form and 7 out of 16 in the S-l form were the same as the corresponding residues of human {alpha}-1-antiproteinase, while 5 of 10 residues in the S-2 form were the same as those of the human inhibitor. Ten out of 16 residues were the same between the F and the S-l forms, whereas the sequence P1 to P'3 of the S-2 form (Tyr-Ser-Met-Pro) was the same as the corresponding residues of mouse {alpha}-1-antiproteinase.


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