Antithrombin is a protease inhibitor that neutralizes the activity of the serine proteases of the
coagulation cascade, such as factors IXa, Xa, XIa, XIIa, and thrombin by forming a 1: 1 …

Heparin has been enzymatically depolymerized with heparinase (heparin lyase (EC 4.2.
2.7)) and then separated into di-, tetra-, hexa-, octa-, and decasaccharide mixtures by low …

Humans express seven heparan sulfate (HS) 3-O-sulfotransferases that differ in substrate
specificity and tissue expression. Although genetic studies have indicated that 3-O-sulfated …

Numerous proteins, including cytokines and chemokines, enzymes and enzyme inhibitors,
extracellular matrix proteins, and membrane receptors, bind heparin. Although they are …

Elucidation of the relationship between the structure and biological function of the
glycosaminoglycans (GAGs) heparin and heparan sulfate (HS) presents an important …

Heparin was discovered around 1922 by Howell (Baltimore) and was further developed by
the teams of Best (Toronto) and Jorpes (Stockholm). Kakkar (London) propagated its routine …

Heparins represent one of the most frequently used pharmacotherapeutics. Discovered
around 1926, routine clinical anticoagulant use of heparin was initiated only after the …

Early structural studies of heparin (Table I) led to the knowledge that heparin binding to AT
produced inhibitory effects against thrombin and factor Xa (2–5). In an effort to obtain …

Revised Manuscript Received May 4, 1993 abstract: An understanding of the substrate
specificity study of the heparin lyases (heparinase and heparitinases) is crucial for …

Samples of heparan sulfate, isolated from bovine aorta, lung, intestine, and kidney, were
degraded by digestion with a mixture of heparitinases or by treatment with nitrous acid, with …