Kirley T L, Wang T, Wallick E T, Lane L K
Biochem Biophys Res Commun. 1985 Jul 31;130(2):732-8. doi: 10.1016/0006-291x(85)90477-2.
Ca2+ and (Na,K)-stimulated ATPases from various species and tissues were labeled with fluorescein isothiocyanate (FITC). Labeled peptides were solubilized by tryptic digestion and purified by reverse phase high pressure liquid chromatography. The amino acid sequences of the labeled peptides reveal considerable homology between sarcoplasmic reticulum Ca2+-ATPases from various sources. These Ca2+-ATPases also contain a region of homology with all other ATPases thus far sequenced. A difference was demonstrated between dog skeletal and cardiac Ca2+-ATPases. These results demonstrate homology of the putative ATP binding site of ATPases, which extends over tissue, species, and cation specificity, including the completely conserved amino acid sequence: lys-gly-ala-pro-glu.
来自不同物种和组织的钙离子(Ca2+)和(钠,钾)刺激的ATP酶用异硫氰酸荧光素(FITC)进行标记。标记的肽段通过胰蛋白酶消化进行溶解,并通过反相高压液相色谱法进行纯化。标记肽段的氨基酸序列显示,来自不同来源的肌浆网Ca2+-ATP酶之间存在相当大的同源性。这些Ca2+-ATP酶还与迄今为止测序的所有其他ATP酶含有一个同源区域。犬类骨骼肌和心肌Ca2+-ATP酶之间存在差异。这些结果证明了ATP酶假定的ATP结合位点的同源性,其跨越组织、物种和阳离子特异性,包括完全保守的氨基酸序列:赖氨酸-甘氨酸-丙氨酸-脯氨酸-谷氨酸。