Glycoproteins enzymatic activities

Coagulation Factors II, III, VII, IX, X, XI, and Xlla fragments, thrombin, and plasmin are classified as serine proteases because each possesses a serine residue with neighboring histidine and asparagine residues at its enzymatically active site (Table 3). Factors II, VII, IX, and X, Protein C, Protein S, and Protein Z are dependent on the presence of vitamin K [84-80-0] for their formation as biologically functionally active procoagulant glycoproteins. 

Hyal-1, an acid-active lysosomal enzyme, was the first somatic hyaluronidase to be isolated and characterized.191,192 It is a 57 kDa single polypeptide glycoprotein that also occurs in a processed 45 kDa form, the result of two endoprotease reactions. The resulting two chains are bound by disulfide bonds. This is not a zymogen-active enzyme relationship, since the two isoforms have similar specific activities. Why two forms should occur is unknown. Only the larger form is present in the circulation, while both isoforms occur in urine,193 in tissue extracts, and in cultured cells. Why an acid-active hyaluronidase should occur in plasma is not clear. Some species do not have detectable enzymatic activity in their circulation,194 but an inactive 70 kDa precursor form of the enzyme is present in such sera, detectable by Western blot (L. Shifrin, M. Neeman, and R. Stern, unpubl. data). Hyal-1 is able to utilize HA of any size as substrate, and generates predominantly tetrasaccharides. 

In addition to the lipid bilayer, enveloped viruses generally have two or more distinct layers of protein that are organized across the membrane. Thus, most viruses have an outer layer of proteins, usually glycoproteins, which are anchored in the membrane as integral membrane proteins. These proteins function to attach the virion to target host cell receptors and facilitate the entry or fusion of the viral membrane with that of the host cell. In addition, some viruses also contain enzymatic activities associated with this outer layer of protein. For example, influenza virus carries with it a neuraminidase that is responsible for cleaving sialic acid residues on host cells. 

Purple acid phosphatases. Diiron-tyrosinate proteins with acid phosphatase activity occur in mammals, plants, and bacteria. Most are basic glycoproteins with an intense 510- to 550-nm light absorption band. Well-studied members come from beef spleen, from the uterine fluid of pregnant sows (uteroferrin), and from human macrophages and osteoclasts. " " One of the two iron atoms is usually in the Fe(III) oxidation state, but the second can be reduced to Fe(II) by mild reductants such as ascorbate. This half-reduced form is enzymatically active and has a pink color and a characteristic EPR signal. Treatment with oxidants such as H2O2 or hexacyannoferrate (III)... 

In addition to staining for total protein, electrophoretic gels can be used for detection of specific protein components. This can be done, for example, by treating the gel in conditions suitable to reveal enzymatic activities, such as chitinolytic (Vincenzi and Curioni, 2005), or staining for glycoproteins with the periodic acid-Schiff method (PAS) (e.g. Marchal et ah, 1996). 

As outlined above, the main drug-metabolizing activity in the gut wall with respect to phase I and phase II enzymes is located in the enterocytes at the tip of the villi. Enzymatic activities of colonocytes, the cells lining the colon, are generally lower however, the expression of apical efflux transport proteins such as P-glycoprotein in colonocytes is significant and exceeds than that in enterocytes (see Chapter 10). 

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