Title : Binding of heparin to human antithrombin III activates selective chemical modification at lysine 236. Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of antithrombin III.

Pub. Date : 1989 Feb 25

PMID : 2492530






8 Functional Relationships(s)
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1 A new water-soluble color reagent, 4-N,N-dimethylaminoazobenzene-4"-isothiocyano-2"-sulfonic acid (S-DABITC), was used to identify lysine residues of antithrombin III which participate in the binding of heparin. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate serpin family C member 1 Homo sapiens
2 Antithrombin, modified with S-DABITC in the presence and absence of low molecular weight heparin (Mr 5000) was reduced, carboxymethylated, and digested with trypsin. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate serpin family C member 1 Homo sapiens
3 When antithrombin was preincubated with heparin (2-fold by weight), followed by S-DABITC modification, the recovery of peptide T4 remained unchanged, but the recoveries of T1, T2, and T3 were reduced by 93, 86, and 98%, respectively. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate serpin family C member 1 Homo sapiens
4 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate serpin family C member 1 Homo sapiens
5 Thus, binding of heparin to human antithrombin diminished S-DABITC modification at Lys-107, Lys-125, and Lys-136, but at the same time enhanced S-DABITC modification at Lys-236. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate serpin family C member 1 Homo sapiens
6 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate serpin family C member 1 Homo sapiens
7 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate serpin family C member 1 Homo sapiens
8 We conclude that Lys-107, Lys-125, and Lys-136 are situated within the heparin-binding site of human antithrombin and that binding of heparin to antithrombin causes a conformational change of antithrombin that leads to the exposure of Lys-236 for S-DABITC modification. 4-(N,N-dimethylaminoazobenzene)-4'-isothiocyanate serpin family C member 1 Homo sapiens