ISSN:
1573-8221
Keywords:
thrombin
;
thymosin
;
platelets
;
blood coagulation
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Abstract A pentapeptide (EEAEN), which is the 24–28 fragment of the COOH-terminal sequence in the thymosinα1 molecule highly homologous with the 54–58 region of hirudin (with the complementary anion-binding exosite in the thrombin molecule), was synthesized by a solid-phase method. Preincubation of α-thrombin with EEAEN in concentrations of 0.1 pM to 1 nM reduced its clotting activity while preincubation of this enzyme with EEAEN in concentrations of 0.01 to 1 nM reduced its platelet-aggregating activity. The reaction of EEAEN with thrombin is shown to be similar to the reaction of the entire thymosinα1 molecule. It is concluded that the COOH-terminal thymosinα1 peptide EEAEN may be the reactive site responsible for the antithrombin activity of thymosinα1.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02444656
