The complete amino acid sequence of ribonuclease from the seeds of bitter gourd (Momordica charantia)

Hiroyuki Ide; Makoto Kimura; Mariko Arai; Gunki Funatsu

doi:10.1016/0014-5793(91)80675-S

The complete amino acid sequence of ribonuclease from the seeds of bitter gourd (Momordica charantia)

Hiroyuki Ide, Makoto Kimura, Mariko Arai, Gunki Funatsu

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

74 Citations (Scopus)

Abstract

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 or 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.

Original language	English
Pages (from-to)	161-164
Number of pages	4
Journal	FEBS Letters
Volume	284
Issue number	2
DOIs	https://doi.org/10.1016/0014-5793(91)80675-S
Publication status	Published - Jun 24 1991

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/0014-5793(91)80675-S

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abstract = "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 or 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.",

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T1 - The complete amino acid sequence of ribonuclease from the seeds of bitter gourd (Momordica charantia)

AU - Ide, Hiroyuki

AU - Kimura, Makoto

AU - Arai, Mariko

AU - Funatsu, Gunki

PY - 1991/6/24

Y1 - 1991/6/24

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AB - 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 or 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.

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The complete amino acid sequence of ribonuclease from the seeds of bitter gourd (Momordica charantia)

Abstract

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