Trypsin inhibitors from bottle gourd (Lagenaria leucantha Rusby var. Depressa Makino) seeds. Purification and amino acid sequences.
Two almost identical trypsin isoinhibitors, LLDTI-I and LLDTI-II, from bottle gourd (Lagenaria leucantha Rusby var. Depressa Makino) seeds were purified by acetone precipitation, gel filtration and reversed phase chromatography. LLDTI-I and LLDTI-II consist of 30 and 29 amino acid residues, respectively, and have identical sequences, except that LLDTI-I has one additional pyroglutamic acid residue at N-terminus. Both proteins are strong inhibitors of bovine trypsin, with Ki values of 2.4.10(-10) M (LLDTI-I) and 9.6.10(-11) M (LLDTI-II). Amino acid sequences are as follows: [sequence: see text]
Matsuo
M
M
Department of Chemistry and Materials Technology, Faculty of Engineering and Design, Kyoto Institute of Technology, Japan.
Hamato
N
N
Takano
R
R
Kamei-Hayashi
K
K
Yasuda-Kamatani
Y
Y
Nomoto
K
K
Hara
S
S
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010944:Plants / Q000737:chemistry*; D012639:Seeds; D016415:Sequence Alignment; D014361:Trypsin Inhibitors / Q000737:chemistry / Q000302:isolation & purification*
D014361:Trypsin Inhibitors