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测定了短小芽孢杆菌碱性蛋白酶BP的分子量为19 500,分析了它的氨基酸组成。用N-溴代琥珀酰亚胺对酶进行了化学修饰,以紫外光谱法测得此酶含有2个色氨酸残基,其中一个残基为酶表现活性的必需基团,且位于分子表面。用荧光表面猝灭剂法推测另一个残基也位于分子表面或临近分子表面。通过其园二色谱证明此酶为无规则卷曲构象。
The molecular weight of Bacillus pumilus alkaline protease BP was determined to be 19 500, and its amino acid composition was analyzed. The enzyme was chemically modified with N-bromosuccinimide and the enzyme contained two tryptophan residues as measured by ultraviolet spectroscopy. One of the residues was an essential group for the enzyme to exhibit activity and was located on the surface of the molecule . Using the fluorescence quencher method to speculate that another residue is also located on or near the molecular surface. The enzyme was proved to be a randomly curled conformation by its circular dichroism.