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Stabilization of molten globule state of papain by urea.
Biochem Biophys Res Commun. 2002 Feb 08; 290(5):1441-6.BB

Abstract

Papain exists in molten globule (MG) state at pH 2.0 and in this state protein tends to aggregate in the presence of lower concentrations of guanidine hydrochloride (GuHC1). Such aggregation is prevented if a low concentration of urea is also present in the buffer; in addition, stabilization of the protein is also induced. Intrinsic fluorescence properties of papain as well as ANS binding suggest significant changes in the structure of papain, in the presence of urea with the absence of major changes in the secondary structure of the protein. The GuHCl- and temperature-induced unfolding of papain, in the presence of urea, indicates stabilization of the protein as seen from the higher transition midpoints, when monitored by fluorescence and circular dichroism (CD). However, a similar phenomenon is not seen under neutral conditions in the presence of urea either at low or high concentrations. The utility of prevention of aggregation by urea is also discussed.

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Authors+Show Affiliations

Edwin F
Molecular Biology Unit, Banaras Hindu University, Varanasi 221 005, India.
Sharma YV
No affiliation info available
Jagannadham MV
No affiliation info available

MeSH

Circular DichroismDose-Response Relationship, DrugDrug StabilityGuanidineHot TemperatureHydrogen-Ion ConcentrationPapainProtein DenaturationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiarySpectrometry, FluorescenceUrea

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

11820783

Citation

Edwin, F, et al. "Stabilization of Molten Globule State of Papain By Urea." Biochemical and Biophysical Research Communications, vol. 290, no. 5, 2002, pp. 1441-6.
Edwin F, Sharma YV, Jagannadham MV. Stabilization of molten globule state of papain by urea. Biochem Biophys Res Commun. 2002;290(5):1441-6.
Edwin, F., Sharma, Y. V., & Jagannadham, M. V. (2002). Stabilization of molten globule state of papain by urea. Biochemical and Biophysical Research Communications, 290(5), 1441-6.
Edwin F, Sharma YV, Jagannadham MV. Stabilization of Molten Globule State of Papain By Urea. Biochem Biophys Res Commun. 2002 Feb 8;290(5):1441-6. PubMed PMID: 11820783.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Stabilization of molten globule state of papain by urea. AU - Edwin,F, AU - Sharma,Yagya Valkya, AU - Jagannadham,M V, PY - 2002/2/1/pubmed PY - 2002/3/16/medline PY - 2002/2/1/entrez SP - 1441 EP - 6 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 290 IS - 5 N2 - Papain exists in molten globule (MG) state at pH 2.0 and in this state protein tends to aggregate in the presence of lower concentrations of guanidine hydrochloride (GuHC1). Such aggregation is prevented if a low concentration of urea is also present in the buffer; in addition, stabilization of the protein is also induced. Intrinsic fluorescence properties of papain as well as ANS binding suggest significant changes in the structure of papain, in the presence of urea with the absence of major changes in the secondary structure of the protein. The GuHCl- and temperature-induced unfolding of papain, in the presence of urea, indicates stabilization of the protein as seen from the higher transition midpoints, when monitored by fluorescence and circular dichroism (CD). However, a similar phenomenon is not seen under neutral conditions in the presence of urea either at low or high concentrations. The utility of prevention of aggregation by urea is also discussed. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/11820783/Stabilization_of_molten_globule_state_of_papain_by_urea_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006291X02963680 DB - PRIME DP - Unbound Medicine ER -