Erzinkyan K L, Trapkov V A, Nizhnii S V, Alaverdyan K G
Biol Bull Acad Sci USSR. 1979 Jan-Feb;6(1):92-4.
The reversible inhibition of the enzymatic activity of trypsin by heparin was investigated. On the basis of an analysis of the Lineweaver-Burk and Dixon graphs, a noncompetitive nature of the inhibition of the BAPA amidase activity of trypsin by heparin was detected, and the values of Km and Ki were determined, equal to 3.1 . 10(-4) and 3.7-3.9 . 10(-7) M, respectively. A comparison of these values indicates a great affinity of heparin for the enzyme. It was shown that heparin inhibits the BAEE esterase activity of trypsin and at the same time has no inhibiting effect on acetyltrypsin. Considering that the acetylation of trypsin leads to selective blocking of the epsilon-amino groups, it was concluded that the epsilon-amino groups of the lysine residues of the trypsin molecule participate in the interaction with heparin.
研究了肝素对胰蛋白酶酶活性的可逆抑制作用。基于对Lineweaver-Burk和Dixon图的分析，检测到肝素对胰蛋白酶BAPA酰胺酶活性的抑制具有非竞争性，并且测定了Km和Ki值，分别等于3.1×10⁻⁴和3.7 - 3.9×10⁻⁷M。这些值的比较表明肝素对该酶具有很强的亲和力。结果表明，肝素抑制胰蛋白酶的BAEE酯酶活性，同时对乙酰胰蛋白酶没有抑制作用。考虑到胰蛋白酶的乙酰化导致ε-氨基的选择性阻断，得出结论：胰蛋白酶分子赖氨酸残基的ε-氨基参与了与肝素的相互作用。
