Mechanism of enhancement of prochymosin renaturation by solubilization of inclusion bodies at alkaline pH

1997 ◽  
Vol 40 (2) ◽  
pp. 169-175 ◽  
Author(s):  
Zhizhou Zhang ◽  
Yuying Zhang ◽  
Kaiyu Yang
Keyword(s):  
Inclusion Bodies ◽  
Alkaline Ph ◽  
Solubilization Of Inclusion Bodies

scholarly journals Denaturation studies on natural and recombinant bovine prochymosin (prorennin)

1990 ◽  
Vol 271 (2) ◽  
pp. 541-547 ◽  
Author(s):  
R Sugrue ◽  
F A O Marston ◽  
P A Lowe ◽  
R B Freedman
Keyword(s):  
Inclusion Bodies ◽  
Kinetic Studies ◽  
Order Rate Constant ◽  
Slow Process ◽  
Equilibrium Studies ◽  
First Order ◽  
Denaturant Concentration ◽  
Recombinant Product ◽  
Stabilization Energies ◽  
Solubilization Of Inclusion Bodies

1. Prochymosin in solution in the presence of 8 M-urea is fully unfolded, as indicated by its fluorescence spectrum, fluorescence quenching behaviour and far-u.v.c.d. spectrum. 2. Equilibrium studies on the unfolding of prochymosin and pepsinogen by urea were carried out at pH 7.5 and pH 9.0. The results indicate that the stabilization energies of the two proteins are identical at pH 7.5, but that at pH 9.0 pepsinogen is significantly less stable than prochymosin. 3. Kinetic studies on the unfolding of prochymosin and pepsinogen indicate that the processes can be described by a single first-order rate constant, and that at any given value of denaturant concentration and pH the rate of unfolding of prochymosin is significantly greater than that of pepsinogen. 4. Unfolding of prochymosin by concentrated urea is not fully reversible, unlike that of pepsinogen. Kinetic analysis of the refolding of the proteins suggests the presence of a slow process following unfolding in urea; for pepsinogen this process leads to a slowly refolding form, whereas for prochymosin the slow process in urea leads to a form that cannot refold on dilution of the denaturant. 5. The results provide a rationale for an empirical process for recovery of recombinant prochymosin after solubilization of inclusion bodies in concentrated urea. 6. In all respects studied here, natural and recombinant bovine prochymosin were indistinguishable, indicating that the refolding protocol yields a recombinant product identical with natural prochymosin.

scholarly journals Microwave assisted solubilization of inclusion bodies

2013 ◽  
Vol 1 (1) ◽  
pp. 2 ◽  
Author(s):  
Ishara Datta ◽  
Saurabh Gautam ◽  
Munishwar N Gupta
Keyword(s):  
Inclusion Bodies ◽  
Microwave Assisted ◽  
Solubilization Of Inclusion Bodies

Efficient solubilization of inclusion bodies

2007 ◽  
Vol 2 (6) ◽  
pp. 678-684 ◽  
Author(s):  
Esteban J. Freydell ◽  
Marcel Ottens ◽  
Michel Eppink ◽  
Gijs van Dedem ◽  
Luuk van der Wielen
Keyword(s):  
Inclusion Bodies ◽  
Solubilization Of Inclusion Bodies

Mechanism and model for solubilization of inclusion bodies

2013 ◽  
Vol 101 ◽  
pp. 631-641 ◽  
Author(s):  
Cornelia Walther ◽  
Sabrina Mayer ◽  
Gerhard Sekot ◽  
Dorota Antos ◽  
Rainer Hahn ◽  
...  
Keyword(s):  
Inclusion Bodies ◽  
Solubilization Of Inclusion Bodies

Non-Denaturing Solubilization of Inclusion Bodies

2010 ◽  
Vol 11 (3) ◽  
pp. 309-312 ◽  
Author(s):  
Kouhei Tsumoto ◽  
Ryota Abe ◽  
Daisuke Ejima ◽  
Tsutomu Arakawa
Keyword(s):  
Inclusion Bodies ◽  
Solubilization Of Inclusion Bodies

scholarly journals Association of high pressure and alkaline condition for solubilization of inclusion bodies and refolding of the NS1 protein from zika virus

2018 ◽  
Vol 18 (1) ◽  
Author(s):  
Cleide Mara Rosa da Silva ◽  
Rosa Maria Chura-Chambi ◽  
Lennon Ramos Pereira ◽  
Yraima Cordeiro ◽  
Luís Carlos de Souza Ferreira ◽  
...  
Keyword(s):  
High Pressure ◽  
Zika Virus ◽  
Inclusion Bodies ◽  
Alkaline Condition ◽  
Ns1 Protein ◽  
Solubilization Of Inclusion Bodies

Inclusion bodies in measles encephalitis

JAMA ◽  
1966 ◽  
Vol 195 (4) ◽  
pp. 307-308
Author(s):  
C. A. Phillips
Keyword(s):  
Inclusion Bodies

Origin of Hepatic Nuclear Inclusion Bodies

1973 ◽  
Vol 31 ◽  
pp. 426-427
Author(s):  
F. G. Zaki ◽  
J. A. Greenlee ◽  
C. H. Keysser
Keyword(s):  
Inclusion Bodies ◽  
Storage Disease ◽  
Glycogen Storage ◽  
Nutritional Deficiencies ◽  
Nuclear Inclusion ◽  
Electron Microscopic ◽  
Human Liver Cells ◽  
Microscopic Studies ◽  
Per Se ◽  
Experimental Liver

Nuclear inclusion bodies seen in human liver cells may appear in light microscopy as deposits of fat or glycogen resulting from various diseases such as diabetes, hepatitis, cholestasis or glycogen storage disease. These deposits have been also encountered in experimental liver injury and in our animals subjected to nutritional deficiencies, drug intoxication and hepatocarcinogens. Sometimes these deposits fail to demonstrate the presence of fat or glycogen and show PAS negative reaction. Such deposits are considered as viral products.Electron microscopic studies of these nuclei revealed that such inclusion bodies were not products of the nucleus per se but were mere segments of endoplasmic reticulum trapped inside invaginating nuclei (Fig. 1-3).

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