Hua J C, Garattini E, Pan Y C, Hulmes J D, Chang M, Brink L, Udenfriend S
Arch Biochem Biophys. 1985 Sep;241(2):380-5. doi: 10.1016/0003-9861(85)90560-0.
Bovine liver alkaline phosphatase has been purified to homogeneity by procedures that include reverse-phase HPLC. The pure enzyme has an apparent Mr of 160,000 and is composed of what appears to be two identical monomers of Mr 82,000. About 80% of the material yielded the amino-terminal sequence Leu-Val-Pro-Glu-Lys-Glu-Lys-Asp-Pro-?-Tyr-?-Arg-Asp-Gln-Ala-Gln. The minor component was extended at the amino terminus by two residues that have not yet been identified, i.e., ?-?-Leu-Val-Pro-Glu-Lys-Glu-Lys-Asp-Pro-?-Tyr-?-Arg-Asp-Gln-Ala-Gln.
通过包括反相高效液相色谱在内的方法,牛肝碱性磷酸酶已被纯化至同质。纯酶的表观分子量为160,000,由两个看似相同的分子量为82,000的单体组成。约80%的材料产生的氨基末端序列为Leu-Val-Pro-Glu-Lys-Glu-Lys-Asp-Pro-?-Tyr-?-Arg-Asp-Gln-Ala-Gln。次要成分在氨基末端延伸了两个尚未鉴定的残基,即?-?-Leu-Val-Pro-Glu-Lys-Glu-Lys-Asp-Pro-?-Tyr-?-Arg-Asp-Gln-Ala-Gln。