Papain: Difference between revisions

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It is a cysteine hydrolase hydrolase that is stable and active under a awide range of conditions. It is very stable even at elevated temperatures(cohen et al. 1986). The latex of Carica papaya is a rich source of four cysteine endopeptidases including papain, chymopapain, glycyl endopeptidase, and caricain. The proteins are synthesized as inactive precursors that become acctive with two minutes of the plant being wounded and the latex expelled. Papain is a minor constituent, but has been more widely studied because it is more easily purified (Azarkan 2003).
It is a [[Cysteine hydrolase|cysteine hydrolase]] that is stable and active under a awide range of conditions. It is very stable even at elevated temperatures <ref>Cohen, L., Coghlan, V and Dihel, L. (1986) Cloning and Sequencing of papain-encoding cDna, Gene 48, 219, 1986</ref>. The [[Latex|latex]] of ''[[Carica papaya|Carica papaya]]'' is a rich source of four [[Cysteine endopeptidases|cysteine endopeptidases]] including papain, [[Chymopapain|chymopapain]], [[Glycyl endopeptidase|glycyl endopeptidase]], and [[Caricain|caricain]]. The proteins are synthesized as inactive precursors that become active with two minutes of the plant being wounded and the latex expelled. Papain is a minor constituent, but has been more widely studied because it is more easily purified <ref>Akahane, K. and Umeyama,H. (1986) Binding Specificity of Papain and Cathepepsin B, Emzyme 36, 141</ref>.<br>


=== Molecular Weight:  ===


*23.4 kDa (theoretical)
*23.0 kDa&nbsp;<ref>Drenth, J., Jansonius, J. Koekoek,R., Swen, H., and Wolters, B.(1968) Structure of Papain, Nature 218, 929</ref><br>


Molecular Weight:
=== Active site residies: ===


*23.4 kDa (theoretical)
*[[Cysteine|cysteine]] (c158)  
*23.0 kDa (Dreuth et al. 1968)
*[[Histidine|histidine]] (h292)  
*[[Asparagine|asparagine]] (n308)<br>


=== Applications:  ===


*Cell isolation where it is more gentle than other [[Proteases|proteases]] (i.e. [[Cortical neurons|cortical neurons]], [[Retina|retina]], and [[Smooth muscle|smooth muscle]])
*Protein structural studies, peptide mapping
*[[Red cells|Red cell]] surface modification for antibody screening or identification
*Fab preparation from [[IgG|IgG]] and [[IgM|IgM]] [[Antibody|antibodies]]
*Solubilization of integral membrane proteins
*Production of [[Glycoproteins|glycopeptides]] from purified [[Proteoglycans|proteoglycans]]
*Enzymatic wound debridement<br>


Active site residies:
=== References ===
 
*cysteine (c158)
*histidine (h292)
*asparagine (n308)<br>
 
 
 
Applications:
 
*cell isolation where it is more gentle than other proteases (i.e.: cortical neurons, retina, and smooth muscle)
*protein structural studies, peptide mapping
*Red cell surface modification for antibody screening or identification
*Fab preparation from IgG and IgM antibodies
*Solubilization of integral membrane proteins
*production og glycopeptides from purified proteoglycans
*Enzymatic wound debridement
 
 
 
 
 
References:
 
Akahane, K. and Umeyama,H. (1986) Binding Specificity of Papain and Cathepepsin B, Emzyme 36, 141
 
 
 
Cohen, L., Coghlan, V and Dihel, L. (1986) Cloning and Sequencing of papain-encoding cDna, Gene 48, 219, 1986
 
 
 
Drenth, J., Jansonius, J. Koekoek,R., Swen, H., and Wolters, B.(1968) Structure of Papain, Nature 218, 929
 


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Latest revision as of 12:50, 28 November 2012

It is a cysteine hydrolase that is stable and active under a awide range of conditions. It is very stable even at elevated temperatures [1]. The latex of Carica papaya is a rich source of four cysteine endopeptidases including papain, chymopapain, glycyl endopeptidase, and caricain. The proteins are synthesized as inactive precursors that become active with two minutes of the plant being wounded and the latex expelled. Papain is a minor constituent, but has been more widely studied because it is more easily purified [2].

Molecular Weight:

  • 23.4 kDa (theoretical)
  • 23.0 kDa [3]

Active site residies:

Applications:

References

  1. Cohen, L., Coghlan, V and Dihel, L. (1986) Cloning and Sequencing of papain-encoding cDna, Gene 48, 219, 1986
  2. Akahane, K. and Umeyama,H. (1986) Binding Specificity of Papain and Cathepepsin B, Emzyme 36, 141
  3. Drenth, J., Jansonius, J. Koekoek,R., Swen, H., and Wolters, B.(1968) Structure of Papain, Nature 218, 929