CRYSTALLIZATION AND PRELIMINARY-X-RAY CHARACTERIZATION OF A SOYBEAN SEED LIPOXYGENASE

被引：19

作者：

STALLINGS, WC

KROA, BA

CARROLL, RT

METZGER, AL

FUNK, MO

机构：

[1] UNIV TOLEDO,DEPT CHEM,TOLEDO,OH 43606

[2] UNIV MICHIGAN,DIV BIOPHYS RES,ANN ARBOR,MI 48109

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1990年 / 211卷 / 04期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

D O I：

10.1016/0022-2836(90)90067-V

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

An isoenzyme of soybean (Glycine max L. Merrill cv. Provar) lipoxygenase (EC 1.13.11.12) has been crystallized using the vapor diffusion method. Crystals were grown from solutions of the protein (7 mg/ml) using 10 to 20% ( w v) polyethylene glycol 8000 in citrate/phosphate buffer (pH 5.7) containing 0.5% ( w v) n-octyl-β-d-glucopyranoside. The crystals reached maximum dimensions of 0.3 mm × 0.2 mm × > 2mm. The enzyme crystallized in space group C2221 with unit cell dimensions a = 246 A ̊, b = 193 A ̊ and c = 75 A ̊. A calculated Vm value of 2.35 Å3/dalton was obtained assuming two molecules per asymmetric unit. The density of the crystals was found to be 1.16 g/ml, which confirmed the presence of two molecules per asymmetric unit and indicated a solvent content of 47.5%. © 1990.

引用

页码：685 / 687

页数：3

共 20 条

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Axelrod B., 1981, METHODS ENZYMOLOGY, P441, DOI DOI 10.1016/0076-6879(81)71055-3

[2] ENZYMATIC LIPOXYGENATION OF ARACHIDONIC-ACID - MECHANISM, INHIBITION, AND ROLE IN EICOSANOID BIOSYNTHESIS [J].