The complete amino acid sequence of ribonuclease from the seeds of bitter gourd (Momordica charantia).
The complete amino acid sequence of ribonuclease (RNase MC) from the seeds of bitter gourd (Momordica charantia) has been determined. This has been achieved by the sequence analysis of peptides derived by enzymatic digestion with trypsin, lysylendopeptidase, and chymotrypsin, as well as by chemical cleavage with cyanogen bromide. The protein contains 191 amino acid residues and has a calculated molecular mass of 21,259 Da. Comparison of this sequence with sequences of the fungal RNases, RNase T2, and RNase Rh, revealed that there are highly conserved residues at positions 32-38 (TXHGLWP) and 81-92 (FWXHEWXKHGTC). Furthermore, the sequence of RNase MC was found to be homologous to those of Nicotiana alata S-glycoproteins involved in self-incompatibility sharing 41% identical residues.
Ide
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Laboratory of Protein Chemistry and Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Kimura
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Arai
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Funatsu
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D000595:Amino Acid Sequence; D002918:Chymotrypsin / Q000378:metabolism; D003488:Cyanogen Bromide; D004722:Endoribonucleases / Q000737:chemistry; D006023:Glycoproteins / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D010947:Plants, Toxic; D012233:Rhizopus / Q000201:enzymology; D012260:Ribonucleases / Q000737:chemistry* / Q000378:metabolism; D012639:Seeds / Q000201:enzymology*; D012689:Sequence Homology, Nucleic Acid; D012697:Serine Endopeptidases / Q000378:metabolism; D014026:Nicotiana / Q000201:enzymology; D014357:Trypsin / Q000378:metabolism
D006023:Glycoproteins; D010446:Peptide Fragments; D004722:Endoribonucleases; D012260:Ribonucleases; C413748:ribonuclease MC1; C022543:ribonuclease T(2); D012697:Serine Endopeptidases; D002918:Chymotrypsin; D014357:Trypsin; C036813:lysyl endopeptidase; D003488:Cyanogen Bromide