晶状体和其他组织中的醛糖还原酶活性

S. Hayman, M.F. Lou, L.O. Merola, J.H. Kinoshita
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引用次数: 80

摘要

1.1. 研究了其醛还原活性在家兔各脏器中的分布。虽然所有研究的器官都有能力使用NADPH作为木糖还原的辅助因子,但观察到的不同底物特异性表明,这种活性可能是由于至少存在两种不同的酶。晶体、肾上腺和骨骼肌中的醛糖还原酶(多元醇:NADP+氧化还原酶,EC 1.1.1.21)和肝脏、肾脏、心脏、脊髓和脑中的NADP+- l -己酸脱氢酶(l - gulate:NADP+氧化还原酶,EC 1.1.1.19)。将小牛晶体解剖成包膜(包括上皮)、皮质和细胞核三部分,测定提取液可溶性部分醛糖还原酶、半乳糖激酶(ATP: d -半乳糖1-磷酸转移酶,EC 2.7.1.6)和葡萄糖-6-磷酸脱氢酶(d -葡萄糖-6-磷酸:NADP+氧化还原酶,EC 1.1.1.49)的浓度。三种酶的分布规律不同:醛糖还原酶的皮质:上皮:细胞核的比值为1:21:1.1;半乳糖激酶为1:3:0.02,葡萄糖-6-磷酸脱氢酶为1:7:0.04。当小牛晶状体在含有半乳糖的培养基中孵育时,dulcitol的积累在上皮区域最多,在细胞核中最少,在皮层中有中等数量。D-[6-14C]-葡萄糖醛酸盐和D-[6-14C]-葡萄糖醛酸内酯在培养兔晶状体中均未合成抗坏血酸。然而,标记的碳转化为CO2,并积累了一些标记的l -谷氨酸盐。醛糖还原酶虽然能将葡萄糖醛酸还原为l -谷氨酸,但似乎不参与抗坏血酸的生物合成。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Aldose reductase activity in the lens and other tissues

  • 1.

    1. The distribution of aldose-reducing activities was studied in several rabbit organs. Although all the organs studied had the ability to use NADPH as a cofactor for the reduction of xylose, the different substrate specificities observed suggest that the activity may be due to the presence of at least two different enzymes. These were aldose reductase (polyol:NADP+ oxidoreductase, EC 1.1.1.21), in lens, adrenal and skeletal muscle and NADP+-L-hexonate dehydrogenase (L-gulonate:NADP+ oxidoreductase, EC 1.1.1.19) in liver, kidney, heart, spinal cord and brain.

  • 2.

    2. Calf lenses were dissected into three portions: capsule (including the epithelium), cortex and nucleus, and the concentrations of aldose reductase, galactokinase, (ATP:D-galactose 1-phosphotransferase, EC 2.7.1.6) and glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate:NADP+ oxidoreductase, EC 1.1.1.49) were determined in the soluble fractions of the extracts. The distribution patterns were different for the three enzymesl the ratio cortex:epithelium:nucleus was 1:21:1.1 for aldose reductase; 1:3:0.02 for galactokinase and 1:7:0.04 for glucose-6-phosphate dehydrogenase.

  • 3.

    3. When calf lenses were incubated in media containing galactose, the accumulation of dulcitol was greatest in the epithelial region and least in the nucleus with an intermediate amount in the cortex.

  • 4.

    4. No biosynthesis of ascorbate from either D-[6-14C]glucuronate or D-[6-14C]-glucuronolactone could be demonstrated in incubated rabbit lens. However, there was conversion of the labeled carbon to CO2 and some accumulation of labeled L-gulonate. Aldose reductase, although it reduces glucuronate to L-gulonate, does not appear to be involved in ascorbate biosynthesis.

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