Wilson J M, O'Toole T E, Argos P, Shewach D S, Daddona P E, Kelley W N
J Biol Chem. 1986 Oct 15;261(29):13677-83.
We defined the amino acid sequence of adenine phosphoribosyltransferase isolated from human erythrocytes. Peptide fragments formed by cleavage at arginine, lysine, glutamic acid, and methionine were purified by high pressure liquid chromatography and sequenced by manual Edman degradation. The complete primary structure of human adenine phosphoribosyltransferase was established by sequence analysis of 19 peptide fragments. Presumed homology between the human and rodent enzymes was used to order fragments that had inadequate overlapping sequences. The enzyme has 179 residues with a calculated subunit molecular weight of 19,481. Mass spectrometry indicated that the NH2-terminal residue is acetylated. Human adenine phosphoribosyltransferase has sequence homology with xanthine-guanine phosphoribosyltransferase from Escherichia coli in 110-amino acid region encompassing the NH2-terminal section of the enzyme.
我们确定了从人红细胞中分离出的腺嘌呤磷酸核糖转移酶的氨基酸序列。通过在精氨酸、赖氨酸、谷氨酸和甲硫氨酸处裂解形成的肽片段，经高压液相色谱法纯化，并通过手动埃德曼降解法测序。通过对19个肽片段的序列分析，确定了人腺嘌呤磷酸核糖转移酶的完整一级结构。利用人与啮齿动物酶之间推测的同源性来排列重叠序列不足的片段。该酶有179个残基，计算出的亚基分子量为19481。质谱分析表明，NH2末端残基被乙酰化。人腺嘌呤磷酸核糖转移酶在包含该酶NH2末端部分的110个氨基酸区域内，与大肠杆菌的黄嘌呤 - 鸟嘌呤磷酸核糖转移酶具有序列同源性。
