Discovery and development of direct thrombin inhibitors the binding site for the globular amino-terminal domain and exosite 1 is the binding site for the acidic carboxy-terminal domain of hirudin. Native hirudin, a 65-amino-acid polypeptide, is produced in the parapharyngeal glands of medicinal leeches. Hirudins today are produced by recombinant biotechnology using yeast. These recombinant hirudins lack a sulfate group at Tyr-63 and are therefore called desulfatohirudins. They have a 10-fold lower binding affinity to thrombin compared to native hirudin, but remain a highly specific inhibitor of thrombin and have an inhibition constant for thrombin in the picomolar range. Renal clearance and degradation account for the most part
Salivary gland in many, but by no means all, bird and mammal species (including humans, as noted above). Furthermore, the venom glands of venomous snakes , Gila monsters, and some shrews, are actually modified salivary glands. In other organisms such as insects, salivary glands are often used to produce biologically important proteins like silk or glues, whilst fly salivary glands contain polytene chromosomes that have been useful in genetic research. Salivary gland The salivary glands in mammals are exocrine glands that produce saliva through a system of ducts. Humans have three paired major salivary glands (parotid, submandibular, and sublingual) as well as