On a Bowman-Birk family proteinase inhibitor from Erythrina variegata seeds.
A Bowman-Birk family proteinase inhibitor (EBI) was isolated from the seeds of Erythrina variegata. The protein was purified by ion-exchange column chromatography on DEAE-cellulose followed by gel filtration on Sephadex G-75. The stoichiometry with trypsin was estimated to be 1:1, while that with chymotrypsin was not obvious, as determined from the titration patterns of its inhibitory activities. The complete amino acid sequence of EBI was determined by sequencing tryptic and chymotryptic peptides. The EBI protein consists of 61 amino acid residues, which is the shortest among the Bowman-Birk family inhibitors sequenced to date, and has a M(r) of 6,689. Comparison of this sequence with those of other leguminous Bowman-Birk family inhibitors revealed that EBI could be classified as a group II inhibitor, showing the best homology (67%) to the Bowman-Birk proteinase inhibitor from soybeans.
Kimura
M
M
Laboratory of Biochemistry, Faculty of Agriculture, Kyushu University, Fukuoka.
Kouzuma
Y
Y
Abe
K
K
Yamasaki
N
N
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D004895:Erythrina / Q000737:chemistry*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010946:Plants, Medicinal; D012639:Seeds / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D014358:Trypsin Inhibitor, Bowman-Birk Soybean / Q000737:chemistry* / Q000145:classification / Q000302:isolation & purification
D000596:Amino Acids; D014358:Trypsin Inhibitor, Bowman-Birk Soybean