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Chymopapain
Chymopapain (, ''chymopapain A'', ''chymopapain B'', ''chymopapain S'', brand name Chymodiactin) is a proteolytic enzyme isolated from the latex of papaya (''Carica papaya''). It is a cysteine protease which belongs to the papain-like protease (PLCP) group. Because of its proteolytic activity, it is the main molecule in the process of chemonucleolysis, used in some procedures like the treatment of herniated lower lumbar discs in the spine by a nonsurgical method. Structure Primary structure Chymopapain's zymogen is made up of a total of 352 residues, and it has a weight of approximately 23.78kDa. Three different regions can be distinguished inside the precursor's chain. * The first 18 aminoacids act as a sorting signal by indicating the final destination of chymopapain inside the cell when being sorted by the Golgi apparatus. Although this final destination is not fully studied yet, other PLCPs are contained in lysosomes and other acidified vesicles and chymopapain is believe ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Caricain
Caricain (, ''papaya peptidase A'', ''papaya peptidase II'', ''papaya proteinase'', ''papaya proteinase III'', ''papaya proteinase 3'', ''proteinase omega'', ''papaya proteinase A'', ''chymopapain S'', ''Pp'') is an enzyme. This enzyme catalysis, catalyses the following chemical reaction: : Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain This enzyme is isolated from the papaya plant, ''Carica papaya''. References External links * {{Portal bar, Biology, border=no EC 3.4.22 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
