Camardella L, Damonte G, Carratore V, Benatti U, Tonetti M, Moneti G
Institute of Protein Biochemistry and Enzymology, C.N.R., Napoli, Italy.
Biochem Biophys Res Commun. 1995 Feb 6;207(1):331-8. doi: 10.1006/bbrc.1995.1192.
Glucose 6-phosphate dehydrogenase from human erythrocytes has a blocked amino-terminus and no information could be obtained by direct sequencing of the intact protein. The peptide corresponding to the amino-terminal region was isolated from a tryptic digest of the whole protein and identified on the basis of its amino acid composition and of the failure to obtain Edman degradation. Determination of peptide mass by fast atom bombardment mass spectrometry allowed identification of the blocked amino-terminal residue as N-acetyl-alanine.
人红细胞中的葡萄糖6-磷酸脱氢酶的氨基末端是封闭的，无法通过对完整蛋白质进行直接测序获得相关信息。从该完整蛋白质的胰蛋白酶消化产物中分离出了与氨基末端区域相对应的肽段，并根据其氨基酸组成以及无法进行埃德曼降解来进行鉴定。通过快速原子轰击质谱法测定肽段质量，从而确定封闭的氨基末端残基为N-乙酰丙氨酸。
