Dispase

Dispase is a protease which cleaves fibronectin, collagen IV, and to a lesser extent collagen I. It is found in some bacteria and can be isolated from culture filtrates of Bacillus polymyxa. It can be extracted, purified, and used in research. It can be particularly useful to separate embryonic epithelia and mesenchyme. Dispase II is specific for the cleavage of leucine-phenylalanine bonds.

Dispase is often used to digest adhering primary cells in culture, since this treatment turned out to be milder than trypsin digestion (Sinclair et al., 2013).

A recent article also finds that dispase can digest serine-phenylalanine.[1]

Dispase intravitreal injection can be used in the modeling of proliferative vitreoretinopathy in different animals.[2][3][4]

## References

[edit]

1. ^ Weimer; et al. (2006). "A quenched fluorescent dipeptide for assaying dispase- and thermolysin-like proteases". Analytical Biochemistry. 352 (1): 110–119\. doi:10.1016/j.ab.2006.02.029. PMID 16564490.
2. ^ Erdiakov AK, Tikhonovich MV, Rzhavina EM, Gavrilova SA (May 2015). "The Characteristics of Retina at the Development of Proliferative Vitreoretinopathy in Rats After Intraocular Injection of Concanavalin a and Dispase". Ross Fiziol Zh Im I M Sechenova. 101 (5): 572–85\. PMID 26263683.
3. ^ Cantó Soler MV, Gallo JE, Dodds RA, Suburo AM (November 2002). "A mouse model of proliferative vitreoretinopathy induced by dispase". Exp Eye Res. 75 (5): 491–504\. doi:10.1006/exer.2002.2031. PMID 12457862.
4. ^ Tikhonovich, Marina V.; Erdiakov, Aleksei K.; Gavrilova, Svetlana A. (2017-06-21). "Nonsteroid anti-inflammatory therapy suppresses the development of proliferative vitreoretinopathy more effectively than a steroid one". International Ophthalmology. 38 (4): 1365–1378\. doi:10.1007/s10792-017-0594-3. ISSN 0165-5701. PMID 28639085.

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Hydrolase: proteases (EC 3.4)

3.4.11-19: Exopeptidase|

| 3.4.11|

* Aminopeptidase
* Alanine
* Arginyl
* Aspartyl
* Cystinyl
* Leucyl
* Glutamyl
* Methionyl
* 1
* 2
* O

|

3.4.13|

* Dipeptidase
* 1
* 2
* 3

3.4.14|

* Dipeptidyl peptidase
* Cathepsin C
* Dipeptidyl peptidase-4
* Tripeptidyl peptidase
* Tripeptidyl peptidase I
* Tripeptidyl peptidase II

3.4.15|

* Angiotensin-converting enzyme

3.4.16|

* Serine type carboxypeptidases: Cathepsin A
* DD-Transpeptidase

3.4.17|

Metalloexopeptidases
Carboxypeptidase

Glutamate II

Other/ungrouped|

* Metalloexopeptidase

3.4.21-25: Endopeptidase|

* Serine protease
* Cysteine protease
* Aspartic acid protease
* Metalloendopeptidase
* Threonine endopeptidase
* Proteasome endopeptidase complex
* HslU—HslV peptidase

* Other/ungrouped: Amyloid precursor protein secretase
* Alpha secretase
* Beta-secretase 1
* Beta-secretase 2
* Gamma secretase

3.4.99: Unknown|

* Staphylokinase

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Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* Cofactor
* Enzyme catalysis

Regulation|

* Allosteric regulation
* Cooperativity
* Enzyme inhibitor
* Enzyme activator

Classification|

* EC number
* Enzyme superfamily
* Enzyme family
* List of enzymes

Kinetics|

* Enzyme kinetics
* Eadie–Hofstee diagram
* Hanes–Woolf plot
* Lineweaver–Burk plot
* Michaelis–Menten kinetics

Types|

* EC1 Oxidoreductases (list)
* EC2 Transferases (list)
* EC3 Hydrolases (list)
* EC4 Lyases (list)
* EC5 Isomerases (list)
* EC6 Ligases (list)
* EC7 Translocases (list)

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