Enzyme factors

Fibrin is formed from fibrinogen synthesized by the liver and secreted into the circulation. The conversion of fibrinogen to fibrin is initiated by a serine protease, thrombin. Thrombin, at the same time, can activate a transglutaminase enzyme, factor XIII present in... 

The production of ligninolytic enzymes takes place during the secondary metabolism of several WRF. The lignin degrading system is induced when starvation of C or N occurs moreover, agitation and temperature can significantly affect the levels of these enzymes factors affecting LMEs are reviewed by Gao et al. [1]. 

The efficiency of the inhibition by a mechanism-based inhibitor depends on the selective addition of the electrophilic entity on a nucleophile of the catalytic site, and not on the other numerous nucleophilic sites of the enzyme. Factors leading to a lack of selectivity are the insufficient reactivity of the electrophilic entity (a long half-life is often accompanied by the diffusion of the species outside the active site) and a large distance between the electrophile and the nucleophile of the active site of the enzyme. 

Nerve Growth (A trypsin-like enzyme Factor activity) with arginine esteropeptidase activity)... 

Thrombin (MW 39,000) is a proteolytic enzyme of the serine protease group. It is derived from prothrombin, a circulating plasma protein, through the proteolytic action of a complex consisting of the proteolytic enzyme factor X (or factor Xa), another protein called factor V (accelerator protein), calcium, and phospholipid. Factor V has recently been identified as the plasma copper protein ceruloplasmin or a similar protein (see Chapter 6). 

A. Blood Clotting Enzyme Factor Xa, FXa, or Factor VIIa, FVIIa Inhibitors... 

V-Guanidinoal kvI amides analogs of the current invention, (n), prepared by Klingler (2) were effective as reversible inhibitors of the blood clotting enzymes factor Xa and/or factor Vila and used in the treatment of thromboembolic diseases or restenosis. 

During blood coagulation either an intrinsic (all blood) system or an extrinsic (tissue juice-lipoprotein) system is activated.. In either case the pathways meet at the activation of Factor X, forming a proteolytic enzyme Factor X. This enzyme in the presence of cofactors (calcium ion, phospholipid and Factor V) will form thrombin from prothrombin. Heparin is a cofactor for a protein called antithrombin III which circulates in the plasma and is an inhibitor of both Factor Xg and thrombin. Antithrombin III neutralizes these 2 enzymes by molecular combination heparin increases the rate of this neutralization. In the past 2 years work has continued on the mechanism of blood coagulation More... 

A6. Ahmed, Z., Abul-Fadl, M. A. M., and King, E. J., The co-enzyme factor of alkaline phosphatase. Biochim. Biophys. Acta 36, 228-240 (1959). 

Enzymes Factor VIII DNase Tissue plasminogen activator... 

Data sources for similar enzymes factor XII (46) heparin (47) Acyl-CoA glucose isomerase ... 

Apparently normal Umbilical vein 199/10 Endothelial line spontaneously transformed immortal has Weibel-Palade bodies and angiotensinconverting enzyme factor VIII negative tumorigenic triploid karyotype (mode 80)... 

Factor VII is a protease. It has been purified from bovine plasma. Unlike factor X and prothrombin it circulates in the plasma as an active enzyme. Factor VII requires a tissue factor before it can exert its proteolytic activity on factor X. 

The clot is stabilized by the formation of covalent bonds introduced by a transglutaminase. Factor Xllla (Lorand et al, 1980 Henschen McDonagh, 1986). The active enzyme. Factor Xllla, is generated from its precursor. Factor XIII, by the action of thrombin (Fi Me 1). The acti dty of Factor Xllla is dependent on both calcium ion concentration and fibrin (ogen). As many as six isopeptide bonds are formed between the side chains of lysine (donor) and glutamine (acceptor) residues. The Y chains of fibrinogen are ligated first, followed by the carboxyl terminal a. chains. The formation of these covalent bonds renders the clot mechanically... 

In the body the oxidation of the heme derived from hemoglobin takes place at the a-methene link, this specific oxidation being brought about by some steric or enzymic factors as yet unknown. Watson and Schwartz have shown that human fistula bile contains bile pigment related primarily to the a-isomers, indicating that it is the a-methene carbon atom which is split out of the porph3rrin ring. 

---