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Publisher Summary This chapter focuses on collagen proline hydroxylase (Rat Skin). In animal tissues, hydroxyproline is found in only one protein, collagen. Although it has long been known that proline is the precursor of hydroxyproline, only recently has it been shown that the hydroxylation of proline occurs in peptide linkage during or after the formation of the polypeptide chains. The enzyme that converts proline residues to hydroxyproline residues, collagen proline hydroxylase, was first found in microsomes and then in the cytoplasmic fraction of chick embryo homogenates. Since then, soluble preparations have been obtained from many tissues of a wide variety of animals. Enzyme preparations have been shown to utilize atmospheric oxygen and to require ascorbate, ferrous ion, and α-ketoglutarate for activity. Certain peptides either biologically or chemically prepared can serve as substrates for collagen proline hydroxylase. Synthetic peptides have been prepared both by random polymerization of tripeptide subunits and by solid-phase synthesis. |
