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The enzyme is deacylated by a water molecule and releases the carboxy terminal portion of the peptide. In immunology, papain is known to cleave the Fc (crystallisable) portion of immunoglobulins (antibodies) from the Fab (antigen-binding) portion. Papain is a relatively heat-resistant enzyme, with an optimal temperature range of 60 to 70 °C. [9]
[3] [10] [9] Many papain-like protease enzymes function as monomers, though a few, such as cathepsin C (Dipeptidyl-peptidase I), are homotetramers. The mature monomer structure is characteristically divided into two lobes or subdomains, known as the L-domain ( N-terminal ) and the R-domain ( C-terminal ), where the active site is located ...
Chymopapain (EC 3.4.22.6, 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. [1]
The enzyme papain can be used to cleave an immunoglobulin monomer into two Fab fragments and an Fc fragment. Conversely, the enzyme pepsin cleaves below the hinge region, so the result instead is a F(ab') 2 fragment and a pFc' fragment. Recently another enzyme for generation of F(ab') 2 has been commercially available.
Discovered by Gopal Chunder Roy in 1873, the first cysteine protease to be isolated and characterized was papain, obtained from Carica papaya. [1] Cysteine proteases are commonly encountered in fruits including the papaya, pineapple, fig and kiwifruit. The proportion of protease tends to be higher when the fruit is unripe.
The nidoviral papain-like protease (PLPro or PLP) is a papain-like protease protein domain encoded in the genomes of nidoviruses.It is expressed as part of a large polyprotein from the ORF1a gene and has cysteine protease enzymatic activity responsible for proteolytic cleavage of some of the N-terminal viral nonstructural proteins within the polyprotein.
The first description of this enzyme was provided by Schack, [1] who named it papaya peptidase A. The same enzyme has since been given a number of different names, including papaya peptidase II, [4] papaya proteinase III [5] and papaya proteinase. [7] The name caricain was recommended by NC-IUBMB in 1992.
Actinidain (EC 3.4.22.14, actinidin, Actinidia anionic protease, proteinase A2 of Actinidia chinensis) is a type of cysteine protease enzyme found in fruits including kiwifruit (genus Actinidia), pineapple, mango, banana, figs, and papaya. This enzyme is part of the peptidase C1 family of papain-like proteases. [1] [2] [3] [4]