查詢結果分析
來源資料
相關文獻
- The Mechanism of Starch Phosphorylase Inhibited by β-Amylase Not in Favor of End-Products Inhibition
- Analysis of β-Amylase Interaction with Starch Phosphorylase Using by Enzyme Kinetics
- Acute Respiratory Failure in Pompe's Disease--A Rare Initial Presentation of a Rare Disease
- The Isolation and Characterization of Chaperonin 60 from Sweet Potato Roots--Involvement of the Chaperonins in Starch Biosynthesis
- 高麥芽糖漿在食品加工中的應用
- 甘藷低糖分性狀的遺傳方式與育種法
- 甘藷癒創組織澱粉磷解酶異構酶之研究
- 甘藷癒創組織澱粉磷解酶異構酶之研究
- Stenotrophomonas Maltophilia Keratitis and Scleritis
- 甘藷之一種澱粉體內酵素--澱粉磷解酶
頁籤選單縮合
題 名 | The Mechanism of Starch Phosphorylase Inhibited by β-Amylase Not in Favor of End-Products Inhibition=終產物抑制理論無法詮釋β-澱粉水解酶抑制澱粉磷解酶的反應 |
---|---|
作 者 | 陳師瑩; | 書刊名 | 嘉南學報 |
卷 期 | 26 2000.11[民89.11] |
頁 次 | 頁122-129 |
分類號 | 346.78 |
關鍵詞 | 澱粉磷解酶; β-澱粉水解酶; 終產物抑制; 麥芽糖; β-極限糊精; Starch phosphorylase; β-Amylase; End-products inhibition; Maltose; β-limit-dextrin; |
語 文 | 英文(English) |
中文摘要 | 由甘藷(Ipomoea batatas [L.] Lam.)中分離出來對澱粉磷解?(SP)具有抑制作用的蛋白質,經鑑定已知為β-澱粉水解?(BA)。為了釐清SP與BA所扮演的生理模糊角色,必需闡明BA抑制SP的分子機轉,其中之一的可能機轉即是終產物抑制理論。因此本實驗的目的即是要證明BA抑制SP的反應中,其終產物所參與的抑制動力學效應。結果顯示,SP具有澱粉及葡萄糖-1-磷酸(G1-P)兩個受質結合位,而麥芽糖和BA的結果相似,與澱粉相互競爭SP的澱粉結合位,而非G1-P之結合位。雖然麥芽糖抑制型態相似於BA,然而根據1%可溶性澱粉經完全水解後所產生的麥芽糖產量,理論上是不足以對SP發生抑制反應。此外β-極限糊精並非作用於SP的澱粉結合位,其抑制型式與BA不同。故結論是麥芽糖與β-極限糊精皆不是造成SP與BA抑制的主因。 |
英文摘要 | The proteinaceous inhibitor of starch phosphorylase (SP) isolated from the root of sweet potato (Ipomoea batatas [L.] Lam.) had been identified as aβ-amylase(BA). For clarifying ambiguities about the physiological roles played by SP and BA, it seems essential to elucidate the molecular mechanism of SP inhibited by BA. One of the possible molecular mechanisms is an end-products inhibition produced by BA. Therefore, the purpose of this study was to demonstrate the inhibitory possibility of end-products produced by BA in the mechanism of SP inhibited by BA used by enzyme kinetics methods. The results indicated that SP had separate binding sites for the two substrates, starch and glucose-1-phosphate (G1-P), and the inhibition of SP by maltose resembling BA was competitive against starch. Therefore, the binding site of either BA or maltose to SP is different from that of G1-P. Although the inhibitory pattern of maltose was similar to BA, it could not inhibit SP unless the theoretical maximum concentration of maltose was attained byβ-amylolysis in a 1% soluble starch. Moreover, the binding site ofβ-limit-dextrin, another end product of BA catalyzation, to SP was different from that of starch and its inhibitory pattern did not match with that of BA. To sum up, neither maltose norβ-limit-dextrin was the major cause for inhibition of SP by BA. |
本系統中英文摘要資訊取自各篇刊載內容。