Allantoinases from bacterial, plant and animal sources I. Purification and enzymic properties

Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation Pub Date : 1966-09-12 DOI:10.1016/0926-6593(66)90040-3

G.D. Vogels, F. Trijbels, A. Uffink

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引用次数: 46

Abstract

1.
1. Allantoinases (allantoin amidohydrolase, EC 3.5.2.5) from Streptococcus allantoicus, Arthrobacter allantoicus, Escherichia coli, Pseudomonas fluorescens, Pseudomonas acidovorans, frog liver, goldfish liver, Phaseolus hysterinus and Glycine hispida were studied.
2.
2. The enzymes were purified 2.5- to 37-fold by (NH₄)₂SO₄ precipitation and DEAE-cellulose chromatography.
3.
3. The pH optimum curve, Michaelis constant, activation energy, stability and specificity were determined and compared.
4.
4. The enzymes from S. allantoicus, A. allantoicus and E. coli were aspecific; the others degraded (+)-allantoin 4–22 times faster than (−)-allantoin.
5.
5. The allantoinases from Ph. hysterinus and G. hispida were activated by acid pretreatment below pH 5.4.

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细菌、植物和动物来源的尿囊酶1 .纯化和酶的性质

1.1. 研究了来自尿囊链球菌、尿囊节杆菌、大肠杆菌、荧光假单胞菌、嗜酸假单胞菌、蛙肝、金鱼肝、宫相虫和甘氨酸的尿囊酶(EC 3.5.2.5)。通过(NH4)2SO4沉淀法和deae -纤维素层析，酶的纯度达到2.5 ~ 37倍。测定并比较了pH最佳曲线、米切里斯常数、活化能、稳定性和特异性。尿囊霉、尿囊霉和大肠杆菌的酶具有特异性;其他菌株降解(+)-尿囊素的速度是(−)-尿囊素的4 ~ 22倍。在pH值低于5.4的条件下，用酸预处理法活化了子宫毛囊酶和毛囊尿囊酶。

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Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation

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