Ide H, Kimura M, Arai M, Funatsu G
Laboratory of Protein Chemistry and Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
FEBS Lett. 1991 Jun 24;284(2):161-4. doi: 10.1016/0014-5793(91)80675-s.
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.
已确定苦瓜（Momordica charantia）种子中核糖核酸酶（RNase MC）的完整氨基酸序列。这是通过对用胰蛋白酶、赖氨酰内肽酶和胰凝乳蛋白酶进行酶切消化以及用溴化氰进行化学裂解得到的肽段进行序列分析来实现的。该蛋白质含有191个氨基酸残基，计算分子量为21,259 Da。将此序列与真菌核糖核酸酶RNase T2和RNase Rh的序列进行比较，发现在32 - 38位（TXHGLWP）和81 - 92位（FWXHEWXKHGTC）存在高度保守的残基。此外，发现RNase MC的序列与参与自交不亲和的烟草S - 糖蛋白的序列同源，有41%的相同残基。
