glu leu gln arg met gln glu lys glu arg asn lys gly gln 100 13 23 leu hse 100 3 gly leu hse 170 ser leu hse 90 100 asn leu hse 90 100 ile leu hse 2 8 ser leu hse 90 100 asn leu hse 90 100 ile leu hse 2 11 glu leu hse 110 asp leu hse 100 2 leu leu hse 100 ile leu hse 100 4 leu leu hse 120 val leu hse 100 10 ile leu hse 110 val leu hse 100 1 tyr 100ile 10 5 tyr leu hse 100 ile leu hse 10 7 phe leu hse 100 ile leu hse 10 19 leu glu hse 90 100 leu asp hse 90 100 22 leu arg hse 90 100 leu lys hse 90 100__________________________________________________________________________ it can be found from the results shown in table 1 that an activity can be increased by exchanging one or more amino acid residues although it has been said that the pharmacological active part of the human motilin depends on amino acid sequence near n terminal the following may be said on the relation between the amino acid sequence near n terminal and a degree of the activity a the motilin analogues wherein pro in 3 position and gly in 8 position of the native motilin are exchanged to gly ser or asn residue which can take a turn structure in the polypeptide chain show the activity in the level same with or.