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Binding protein-enzyme complex

Adenosine deaminase (ADA) is an amino hydrolase that catalyzes the deamination of adenosine and 2 -deoxyadenosine to inosine and 2 -deoxyinosine, respectively. High activity of ADA is seen in thymus and other lymphoid tissues. ADA has been shown in many different physical forms. A small form of the enzyme predominates in the spleen, stomach, and red blood cells, whereas the large form predominates in the kidney, liver, and skin fibroblasts. The small form of the catalytic subunit can be converted to the large form by complexing with a protein termed binding protein or complexing protein. [Pg.14]

An example for proteases are the (3-lactamases that hydrolyse a peptide bond in the essential (3-lactam ring of penicillins, cephalosporins, carbapenems and monobac-tams and, thereby, iireversibly inactivate the diug. 13-lactamases share this mechanism with the penicillin binding proteins (PBPs), which are essential enzymes catalyzing the biosynthesis of the bacterial cell wall. In contrast to the PBPs which irreversibly bind (3-lactams to the active site serine, the analogous complex of the diug with (3-lactamases is rapidly hydrolyzed regenerating the enzyme for inactivation of additional (3-lactam molecules. [Pg.103]

Ca2+-pumps. After entering the cell, Ca2+ is reversibly complexed to specific Ca2+-binding proteins that fiilfil multiple functions, including Ca2+-buffering and transport, activation of enzymes, regulation of contraction,... [Pg.1103]

Calcium-binding proteins, 6, 564, 572, 596 intestinal, 6, 576 structure, 6, 573 Calcium carbonate calcium deposition as, 6, 597 Calcium complexes acetylacetone, 2, 372 amides, 2,164 amino acids, 3, 33 arsine oxides, 3, 9 biology, 6, 549 bipyridyl, 3, 13 crown ethers, 3, 39 dimethylphthalate, 3, 16 enzyme stabilization, 6, 549 hydrates, 3, 7 ionophores, 3, 66 malonic acid, 2, 444 peptides, 3, 33 phosphines, 3, 9 phthalocyanines, 2,863 porphyrins, 2, 820 proteins, 2, 770 pyridine oxide, 3,9 Schiff bases, 3, 29 urea, 3, 9... [Pg.97]

In general, the receptor-G-proteins complexes exchange bound GDP for GTP. In turn, the two, smaller subunits of the G-protein components of these complexes are released and the receptor protein dissociates. The remaining G-protein GTP complex then complexes with and activates a specific enzyme. It is very significant to note that G-proteins therefore have at least three specific binding sites (a) for nucleotides, (b) for a receptor protein, and (c) an effector protein. [Pg.191]

KDHRF A homologous restriction factor binds to C8 65KDHRF A homologous restriction factor, also known as C8 binding protein interferes with cell membrane pore-formation by C5b-C8 complex Kcat Catalytic constant a measure of the catalytic potential of an enzyme Ka Equilibrium dissociation constant kD Kilodalton Kd Dissociation constant KD Kallidin... [Pg.283]

It should be pointed out that the addition of substances, which could improve the biocompatibility of sol-gel processing and the functional characteristics of the silica matrix, is practiced rather widely. Polyethylene glycol) is one of such additives [110— 113]. Enzyme stabilization was favored by formation of polyelectrolyte complexes with polymers. For example, an increase in the lactate oxidase and glycolate oxidase activity and lifetime took place when they were combined with poly(N-vinylimida-zole) and poly(ethyleneimine), respectively, prior to their immobilization [87,114]. To improve the functional efficiency of entrapped horseradish peroxidase, a graft copolymer of polyvinylimidazole and polyvinylpyridine was added [115,116]. As shown in Refs. [117,118], the denaturation of calcium-binding proteins, cod III parvalbumin and oncomodulin, in the course of sol-gel processing could be decreased by complexation with calcium cations. [Pg.85]


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Complex proteins

Enzymes binding

Protein complexity

Protein-enzyme complexes

Proteins complexation

Proteins enzymes

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