The Mechanism of Starch Phosphorylase Inhibited by β-Amylase Not in Favor of End-Product Inhibition

Chia Nan University of Pharmacy & Science Institutional Repository > 嘉南學報 > 26 期 (2000) > Item 310902800/22382

jsp.display-item.identifier=請使用永久網址來引用或連結此文件: https://ir.cnu.edu.tw/handle/310902800/22382

標題:	The Mechanism of Starch Phosphorylase Inhibited by β-Amylase Not in Favor of End-Product 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:	Shih-Ying Chen
貢獻者:	保健營養系
關鍵字:	Starch phosphorylase β-Amylase end-products inhibition maltose β-limit-dextrin 澱粉磷解酶 β-澱粉水解酶終產物抑制麥芽糖 β-極限糊精
日期:	2000
上傳時間:	2010-03-22 11:23:16 (UTC+8)
摘要:	The proteinaceous inhibitor of starch phosphorylase (SP) isolated from the root of sweet potato (Ipomoea batatas [L.] Lam.) had been identified as a β-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 producted by BA. Therefore,the purpose of this study was to demonstrate the inhibitory possibitory 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 by β- amylolysis in a 1% soluble starch. Moreover, the binding site of β-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 nor β-limit-dextrin was the major cause forinhibition of SP by BA.
關聯:	嘉南學報 26 ：p.122-129
显示于类别:	[嘉南學報] 26 期 (2000) [保健營養系(所) ] 期刊論文

文件中的档案:

没有与此文件相关的档案.

在CNU IR中所有的数据项都受到原著作权保护.

TAIR相关文章

数据加载中.....