Hementin is an anticoagulant protease from the salivary glands of the giant Amazon leech (Haementeria ghilianii). Hementin dissolves a type of platelet rich blood clot which cannot be dissolved by other well used drugs like streptokinase and urokinase.
Hementin is a calcium-dependent protease with a molecular weight of 80-120 kDa. It is capable of disrupting the function of fibrinogen, a glycoprotein responsible for blood clotting, by cleaving three peptide bonds in its structure. Fibrinogen acts as a substrate for thrombin, which converts the protein into its functional form, fibrin. Cleavage of fibrinogen in its native conformation at Asn102-Asn103, Lys130-Gln131, and Pro76-Asn77 yield three sets of products. Hementin may also cause platelet deaggregation, although such effects are not as emphasized as its proteolytic capabilities. Because of its anticoagulant effects, Hementin can be described as a hemostatic regulator.
- Budzynski, A. Z. (February 1991). "Interaction of hementin with fibrinogen and fibrin". Blood Coagulation & Fibrinolysis. 2 (1): 149–152. doi:10.1097/00001721-199102000-00022. ISSN 0957-5235. PMID 1772982.
- Zavalova, L. L.; Basanova, A. V.; Baskova, I. P. (2002). "Fibrinogen–Fibrin System Regulators from Bloodsuckers". Biochemistry (Moscow). 67 (1): 135–142. doi:10.1023/A:1013916601281.
- Malinconico, SM; Katz, JB; Budzynski, AZ (January 1984). "Hementin: anticoagulant protease from the salivary gland of the leech Haementeria ghilianii". The Journal of Laboratory and Clinical Medicine. 103 (1): 44–58. PMID 6361187.
|This biochemistry article is a stub. You can help Wikipedia by expanding it.|