METABOLISM OF TREHALOSE IN EUGLENA-GRACILIS - PARTIAL-PURIFICATION AND SOME PROPERTIES OF PHOSPHOGLUCOMUTASE ACTING ON BETA-GLUCOSE 1-PHOSPHATE
METABOLISM OF TREHALOSE IN EUGLENA-GRACILIS - PARTIAL-PURIFICATION AND SOME PROPERTIES OF PHOSPHOGLUCOMUTASE ACTING ON BETA-GLUCOSE 1-PHOSPHATE
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DOI：
10.1111/j.1432-1033.1974.tb03659.x
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发表时间：
1974-01-01
期刊：
影响因子：
--
通讯作者：
MARECHAL, LR
中科院分区：
文献类型：
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作者：
BELOCOPITOW, E;MARECHAL, LR
β-葡萄糖1-磷酸磷酸葡萄糖变位酶是一种存在于纤细裸藻杆状变种无细胞提取物中的酶，可催化β-葡萄糖1-磷酸可逆转化为葡萄糖6-磷酸。通过硫酸鱼精蛋白处理、Sephadex G-100凝胶过滤和DEAE-纤维素柱层析，将其纯化460倍。反应的最适pH为7.0，平衡常数β-葡萄糖1-磷酸/葡萄糖6-磷酸为0.035。该酶绝对需要β-葡萄糖1，6-二磷酸以及二价阳离子，如Mg 2+、Co2+或Mn 2+。经SephadexG-100凝胶电泳测定，其表观分子量约为27000。该酶与存在于同一眼虫提取物中的海藻糖磷酸化酶共同构成了一条新的海藻糖分解代谢途径，并讨论了α-和β-葡萄糖1，6-二磷酸在眼虫能量代谢系统中的调节作用。
Phosphoglucomutase for β‐glucose 1‐phosphate, an enzyme present in cell‐free extracts ofEuglena gracilisvar.bacillaris, catalyzes the reversible conversion of β‐glucose 1‐phosphate to glucose 6‐phosphate. It was purified 460‐fold by treatment with protamine sulphate, gel filtration in Sephadex G‐100 and chromatography on a DEAE‐cellulose column. The optimum pH of the reaction was 7.0 and the equilibrium constant β‐glucose 1‐phosphate/glucose 6‐phosphate was 0.035. The enzyme has an absolute requirement for β‐glucose 1,6‐bisphosphate as well as a bivalent cation such as Mg2+, Co2+or Mn2+. Measurements in Sephadex G‐100 gave an apparent molecular weight of about 27000.This enzyme together with a trehalose phosphorylase found in the sameEuglenaextracts would constitute a new catabolic pathway for trehalose.The functions of α‐ and β‐glucose 1,6‐bisphosphate as regulation factors in the energy furnisher system inEuglenais discussed.