High impact information on LOC396443

• These findings suggest that ovalbumin does not undergo a marked conformational change analogous to that inferred for the related members of the serpin superfamily, alpha 1-antitrypsin and antithrombin III, nor do the residues close to the site of proteolysis appear to change environment from that of an exposed loop to a buried strand of beta-sheet [1].
• This activity is similar to that of C1-inhibitor but different from antithrombin III, alpha 2-antiplasmin, or alpha 1-protease inhibitor [2].
• Intron structure of the human antithrombin III gene differs from that of other members of the serine protease inhibitor superfamily [3].
• Location of two of the introns in the antithrombin-III gene [4].
• The pharmacological activities of 14 heparins prepared from bovine and hog tissues and heparin fractions obtained by molecular sieving on sephacryl S-200 and antithrombin III affinity chromatography are reported [5].

Biological context of LOC396443

• Compared with controls, intoxicated chicks exhibited decreased prothrombin time, increased plasma fibrinogen (not included for the group receiving 30 mg/kg of culture material), and increased antithrombin III activity [6].
• Antithrombin III is the principal circulating active-site inhibitor of thrombin and other serine proteinases [7].

Anatomical context of LOC396443

• Evidence that chicken antithrombin III is a developmentally regulated glycoprotein synthesized by hepatocytes [7].
• We studied a protein synthesized and secreted by cultured chick embryo hepatocytes that has very similar immunological, structural and functional properties to adult antithrombin III [7].

Associations of LOC396443 with chemical compounds

• Consistent with this finding, embryonic plasma antithrombin III had no sialic acid (less than 0.01 residue/mol) in contrast with the adult form (3.5 residues/mol) [7].
• Antithrombin III antigen levels were increased 3- to 4-fold in the presence of dexamethasone (2 nM) during a 3-day culture period [7].

References