犊牛肠碱性磷酸酶活性丝氨酸周围的氨基酸序列

Lorents Engström
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引用次数: 25

摘要

二肽Asp-SER32P和Ser32P-Ala是从小牛肠碱性磷酸盐(正磷酸单酯磷酸水解酶,EC 3.I.3.I)的酸水解产物中分离出来的,如前所述,二肽在活性位点的丝氨酸残基上进行了32p标记。这表明活性丝氨酸周围的氨基酸序列为ASP-Ser32P-Ala。用酸水解结晶卵清蛋白鉴定肽,同样的非球化肽作为对照物质。
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The amino acid sequence around the reactive serine in calf-intestinal alkaline phosphatase

The dipeptides Asp-SER32P and Ser32P-Ala have been isolated from an acid hydrolysate of calf-intestinal alkaline phosphate (orthophosphoric monoester phosphohydrolase, EC 3.I.3.I), which had been 32P-labelled on a serine residue at the active site, as described earlier. This shows that the amino acid sequence aroun the active serine is ASP-Ser32P-Ala. The peptides were identified by using an acid hydrolysate of crytalline ovalbumin the same unballed peptides as reference substances.

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