The cleavage reactions of Ser-His and its N-terminal phosphorylated form - N-(O.O-diisopropyl) phosphoryl seryl-histidine (DIPP-Ser-His) were studied on DNA. It was found that the phosporylation of Ser-His caused the ...The cleavage reactions of Ser-His and its N-terminal phosphorylated form - N-(O.O-diisopropyl) phosphoryl seryl-histidine (DIPP-Ser-His) were studied on DNA. It was found that the phosporylation of Ser-His caused the lost of the cleavage activity on DNA. The result might give some clue on the regulation of the activity of protein by展开更多
The cleavage activity of histidine on RNA and DNA was tested. It was found that histidine could cleave RNA, but not DNA. The cleavage mechanism was proposed to be involved in the hydrolysis of the phosphodiester
In the presence of histidine N -(O, O-diisopropyl)phosphoryl serine could catalyze the cleavage of RNA in aqueous solution at neutral pH. The results were detected by sub-marine agarose gel electrophoresis and capilla...In the presence of histidine N -(O, O-diisopropyl)phosphoryl serine could catalyze the cleavage of RNA in aqueous solution at neutral pH. The results were detected by sub-marine agarose gel electrophoresis and capillary zone electrophoresis. It uas found that at high concentration histidine could cleave the RNA slightly. While the participation of DIPP-Ser could significantly accelerate the cleavage reaction. N-phosphodipeptidede ---N -(O. O-diisopropyl)phosphoryl Ser-His are proposed to be involved in the mechanism.展开更多
The cleavage activity of histidyl-lysine dipeptide (His-Lys) on RNA was studied and compared with that of histidine. With the addition of the lysine residue, the cleavage activity was increased about 10-fold compared ...The cleavage activity of histidyl-lysine dipeptide (His-Lys) on RNA was studied and compared with that of histidine. With the addition of the lysine residue, the cleavage activity was increased about 10-fold compared to that of histidine. The cleavage mechanism of His-Lys was also discussed.展开更多
文摘The cleavage reactions of Ser-His and its N-terminal phosphorylated form - N-(O.O-diisopropyl) phosphoryl seryl-histidine (DIPP-Ser-His) were studied on DNA. It was found that the phosporylation of Ser-His caused the lost of the cleavage activity on DNA. The result might give some clue on the regulation of the activity of protein by
文摘The cleavage activity of histidine on RNA and DNA was tested. It was found that histidine could cleave RNA, but not DNA. The cleavage mechanism was proposed to be involved in the hydrolysis of the phosphodiester
文摘In the presence of histidine N -(O, O-diisopropyl)phosphoryl serine could catalyze the cleavage of RNA in aqueous solution at neutral pH. The results were detected by sub-marine agarose gel electrophoresis and capillary zone electrophoresis. It uas found that at high concentration histidine could cleave the RNA slightly. While the participation of DIPP-Ser could significantly accelerate the cleavage reaction. N-phosphodipeptidede ---N -(O. O-diisopropyl)phosphoryl Ser-His are proposed to be involved in the mechanism.
文摘The cleavage activity of histidyl-lysine dipeptide (His-Lys) on RNA was studied and compared with that of histidine. With the addition of the lysine residue, the cleavage activity was increased about 10-fold compared to that of histidine. The cleavage mechanism of His-Lys was also discussed.
