来自大肠杆菌的羟甲基胆色素原合酶（胆色素原脱氨酶）的纯化、N端氨基酸序列及性质
Purification, N-terminal amino acid sequence and properties of hydroxymethylbilane synthase (porphobilinogen deaminase) from Escherichia coli.
作者信息
Hart G J, Abell C, Battersby A R
出版信息
Biochem J. 1986 Nov 15;240(1):273-6. doi: 10.1042/bj2400273.
Abstract
Hydroxymethylbilane synthase (porphobilinogen deaminase) was purified to apparent homogeneity from Escherichia coli. The enzyme is a monomer of Mr approx. 40,000. The Km for porphobilinogen and relative Vmax. values have been obtained at various pH values over the range 6.2-8.8, enabling pK values for ionizable groups important for activity to be determined. The N-terminal amino acid sequence is presented.
摘要
从大肠杆菌中纯化出了羟甲基胆色素原合酶（胆色素原脱氨酶），达到了表观均一性。该酶是一种分子量约为40,000的单体。已在6.2 - 8.8的不同pH值下获得了胆色素原的米氏常数（Km）和相对最大反应速度（Vmax）值，从而能够确定对活性重要的可电离基团的pK值。给出了N端氨基酸序列。
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