TY - JOUR
T1 - The Complete Amino Acid Sequence of Antiviral Protein from the Seeds of Pokeweed (Phytolacca americana)
AU - Kung, Sung Sil
AU - Kimura, Makoto
AU - Funatsu, Gunki
N1 - Funding Information:
Materials. TPCK-trypsin, TLCK-chymotrypsin, and pepsin were purchased from Sigma Chemical Co. Lysylendopeptidase from Achromobacter lyticus, cyanogen bromide, and succinic anhydride were from Wako Pure Chemicals. All reagents used were of analytical grade. PAP-S was prepared from a low-pH extract of the seeds by DEAE-and CM-cellulose column chromatography 1 This work was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan. tt To whom correspondence should be addressed. Abbreviations: CNBr, cyanogen bromide; RP-HPLC, reverse-phase high-performance liquid chromatography; TFA, trifuoroacetic acid; SDS-PAGE, SDS-polyacrylamide gel electrophoresis; DABITC/PITC, 4-N,N-dimethylaminoazobenzene-4-isothiocyanate/phenylisothiocyanate.
PY - 1990
Y1 - 1990
N2 - The complete amino acid sequence of antiviral protein from the seeds of pokeweed (Phytolacca americana) has been determined. This has been done by the sequence analysis of peptides derived by enzymatic digestion with trypsin, pepsin, and Iysylendopeptidase, as well as by chemical cleavage with cyanogen bromide. The protein consists of 261 amino acid residues containing two disulfide bonds and has a calculated molecular mass of 29167 Da. The two disulfide bonds connect Cys-34 to Cys-258 and Cys-84 to Cys-105. Comparison of this sequence with the sequence of the ricin A-chain shows that there are identical residues at 76 positions in the two molecules (30% identity), having an extended region of highly conserved sequence at positions 170-183 (IQMXSEAARFXYIE). In contrast, the internal regions at positions 77 119 and 141 169 and the C-terminal 15 amino acid residues are less homologous in the two proteins.
AB - The complete amino acid sequence of antiviral protein from the seeds of pokeweed (Phytolacca americana) has been determined. This has been done by the sequence analysis of peptides derived by enzymatic digestion with trypsin, pepsin, and Iysylendopeptidase, as well as by chemical cleavage with cyanogen bromide. The protein consists of 261 amino acid residues containing two disulfide bonds and has a calculated molecular mass of 29167 Da. The two disulfide bonds connect Cys-34 to Cys-258 and Cys-84 to Cys-105. Comparison of this sequence with the sequence of the ricin A-chain shows that there are identical residues at 76 positions in the two molecules (30% identity), having an extended region of highly conserved sequence at positions 170-183 (IQMXSEAARFXYIE). In contrast, the internal regions at positions 77 119 and 141 169 and the C-terminal 15 amino acid residues are less homologous in the two proteins.
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U2 - 10.1271/bbb1961.54.3301
DO - 10.1271/bbb1961.54.3301
M3 - Article
C2 - 1368643
AN - SCOPUS:0025583408
SN - 0002-1369
VL - 54
SP - 3301
EP - 3318
JO - Agricultural and Biological Chemistry
JF - Agricultural and Biological Chemistry
IS - 12
ER -