Collagen enzyme

Preparation of Collagen-Enzyme Complexes. Collagen-enzyme complexes were prepared by the membrane impregnation method (9,... 

Enzyme Binding Capacity Determination. Two steps or stages are involved in formation of a stable collagen/enzyme complex. 

Helicity is one of the subdest aspects of polymer chain where the polymer chain spiral structure along the chain axis acts like a spring. Helical polymers are frequently occurring in nature in single, double or triple helices form in genes, proteins, DNA, collagen, enzymes, and polypeptides. The stability of natural polypeptides are increased due to the helical confirmations. 

FIGURE 6.20 A disaccharide of galactose and glucose is covalently linked to the 5-hydroxyl group of hydroxylysines in collagen by the combined action of the enzymes galactosyl transferase and glucosyl transferase. 

The enzyme is used in an enzyme electrode in which a tube is sealed at its lower end with a cellulose acetate membrane. An outer membrane of collagen is also attached to the end of the electrode tube and glucose oxidase enzyme is contained in the space between the two diaphragms. 

FIGURE 6-2 Steps in the preparation of an ainperometric enzyme electrode with simple enzyme immohilization hy trapping between an inner cellulose acetate and outer collagen membrane, cast on the electrode body. (Reproduced with permission from reference 1.)... 

Carnivores rely on a protein-rich diet and produce new biomass primarily from dietary amino acids, although the enzymes required for de novo amino acid synthesis are present (Garmes et al., 1998). Bone collagen, muscle (meat) and apatite were analyzed for a set of modern southern African herbivores and carnivores (Lee-Thorp et al., 1989). The isotopic analyses showed i C enrichment in bone collagen, apatite and muscle, and depletion in lipids. Difference in values between herbivores and carnivores indicates a trophic effect, which for carbon in bone collagen is 2.5-3%o (Fig. 2). 

A number of iron-containing, ascorbate-requiring hydroxylases share a common reaction mechanism in which hydroxylation of the substrate is linked to decarboxylation of a-ketoglutarate (Figure 28-11). Many of these enzymes are involved in the modification of precursor proteins. Proline and lysine hydroxylases are required for the postsynthetic modification of procollagen to collagen, and prohne hydroxylase is also required in formation of osteocalcin and the Clq component of complement. Aspartate P-hydroxylase is required for the postsynthetic modification of the precursor of protein C, the vitamin K-dependent protease which hydrolyzes activated factor V in the blood clotting cascade. TrimethyUysine and y-butyrobetaine hydroxylases are required for the synthesis of carnitine. 

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