【摘 要】
：
The trypsin inhibitor from mung bean has a molecular weight of 7984, consisting of two active domains and seven disulfide bonds. It belongs to the Bowman-Birk
【机 构】
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Shanghai Institute of Biochemistry, Academia Sinicarrrrrrrrn,Shanghai Institute of Biochemi
【出 处】
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Science in China,Ser.B
论文部分内容阅读
The trypsin inhibitor from mung bean has a molecular weight of 7984, consisting of two active domains and seven disulfide bonds. It belongs to the Bowman-Birk inhibitor. This inhibitor has been crystallized in two crystalline forms either by dialysis or by batch method. One is tetragonal with unit cell of symmetry P4_122(or P4_322) and dimensions a=b=49.21, c=158.07, each asymmetric unit containing three molecules. Another is orthorhombic with unit cell of symmetry P2_12_12 and dimensions a=39.65, b=57.18, c=52.02, each asymmetric unit containing two molecules.
The trypsin inhibitor from mung bean has a molecular weight of 7984, consisting of two active domains and seven disulfide bonds. It belongs to the Bowman-Birk inhibitor. This inhibitor has been crystallized in two crystalline forms either by dialysis or by batch method. One is tetragonal with unit cell of symmetry P4_122 (or P4_322) and dimensions a = b = 49.21, c = 158.07, each asymmetric unit contains three molecules. Another is orthorhombic with unit cell of symmetry P2_12_12 and dimensions a = 39.65, b = 57.18, c = 52.02, each asymmetric unit contains two molecules.
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