THE PHOSPHORYLATION SITE OF SNAKE MUSCLE FRUCTOSE 1,6-BISPHOSPHATASE AND ITS PHOSPHORYLATION CONDITIONS |
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作者姓名: | 胡国富 许根俊 |
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作者单位: | Shanghai Institute of Biochemistry,Academia Sinica,Shanghai Institute of Biochemistry,Academia Sinica |
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基金项目: | Project supported by the National Natural Science Foundation of China. |
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摘 要: | From the tryptic digests of phosphorylated snake muscle FruP_(2ase), a phosphoryl peptide has beenisolated, its amino acid sequence was Gly-Ala-Gly-Ser-Arg and the phosphorylation site was consideredto be on the serine residue. Effectors of the enzyme such as FruP_2, F6P and AMP did not affect thephosphorylation. The effect of pH on phosphorylation was consistent with that on the activity of theenzyme. The activity of phosphorylated enzyme was slightly lower than that of the native enzyme, thisdifference in activities between the two forms of the enzyme increased with decreasing the substrateconcentration. Results further support that a phosphorylated intermediate is involved in the catalytic reac-tion of FruP_(2ase).
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