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Journal articles on the topic 'Lysozyme; Trifluoroethanol; Guanidinium chloride'

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Published: 4 June 2021
Last updated: 11 February 2022

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1

Sasahara, Kenji, and Katsutoshi Nitta. "Pressure-induced unfolding of lysozyme in aqueous guanidinium chloride solution." Protein Science 8, no. 7 (1999): 1469–74. http://dx.doi.org/10.1110/ps.8.7.1469.

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2

Duan, Haiyan, Xiandong Zeng, Biyu Tang, Xiaotao Liu, Guohua Lan, Wanzhi Wei, and Shenglian Luo. "Cooperative Effect of Guanidinium Chloride and Urea on Lysozyme Refolding." Analytical Letters 42, no. 16 (October 30, 2009): 2625–36. http://dx.doi.org/10.1080/00032710903243596.

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3

Field, J. M., A. S. Tatham, and P. R. Shewry. "The structure of a high-Mr subunit of durum-wheat (Triticum durum) gluten." Biochemical Journal 247, no. 1 (October 1, 1987): 215–21. http://dx.doi.org/10.1042/bj2470215.

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A high-Mr subunit was prepared from durum wheat (Triticum durum). Viscometric analysis showed that the molecule is rod-shaped, with molecular dimensions of about 50 nm x 1.75 nm (500 A x 17.5 A) in 0.05 M-acetic acid/0.01 M-glycine and 49 nm x 1.79 nm (490 A x 17.9 A) in aq. 50% (v/v) propan-1-ol (+/- 0.01 M-glycine) at 30 degrees C. C.d. spectroscopy in the same solvents indicated the presence of beta-turns, but little alpha-helix [7% in 50% (v/v) propan-1-ol] and no beta-sheet. However, when dissolved in trifluoroethanol the protein contains about 30% alpha-helix, and viscometric analysis gives dimensions of about 62 nm x 1.53 nm (620 A x 15.3 A). It is proposed, on the basis of these studies and previously published structural prediction, that the repetitive central domain of the high-Mr subunit forms a loose spiral based on repetitive beta-turns, whereas the shorter non-repetitive N- and C-terminal domains are alpha-helical in trifluoroethanol, but random coil in other solvents. The Mr of the high-Mr subunit determined from the intrinsic viscosity in 6.0 M-guanidinium chloride was 65,000, compared with 84,000 determined in 5.0 M-guanidinium thiocyanate. The latter value is consistent with the Mr values for related proteins whose complete amino acid sequences are known, and it was concluded that the protein is incompletely denatured in the former solvent. This was confirmed by c.d. spectroscopy in increasing concentrations (1-6 M) of guanidinium chloride.
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4

Ahmad, F., S. Yadav, and S. Taneja. "Determining stability of proteins from guanidinium chloride transition curves." Biochemical Journal 287, no. 2 (October 15, 1992): 481–85. http://dx.doi.org/10.1042/bj2870481.

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The guanidinium chloride (GdmCl) denaturation of RNAase A, lysozyme and metmyoglobin was investigated at several pH values by using absorbance measurements at 287, 300 and 409 nm respectively. From these measurements the free-energy change on denaturation, delta Gapp., was calculated, assuming a two-state mechanism, and values of delta Gapp. at zero concentration of the denaturant were measured. For each protein all delta Gapp. values were adjusted to pH 7.00 by using the appropriate relationship between delta Gapp. and pH. Dependence of the adjusted delta Gapp. value on GdmCl concentration increases for metmyoglobin and decreases for the other two proteins as the denaturant concentration decreases. It has been shown that these are expected results if the presence of the acid-denatured state during the GdmCl denaturation of proteins is considered.
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5

Kotik, Michael, Sheena E. Radford, and Christopher M. Dobson. "Comparison of the Refolding Hen Lysozyme from Dimethyl Sulfoxide and Guanidinium Chloride." Biochemistry 34, no. 5 (February 1995): 1714–24. http://dx.doi.org/10.1021/bi00005a028.

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6

Lyster, Richard L. J. "Effect of calcium on the stability of mares' milk lysozyme." Journal of Dairy Research 59, no. 3 (August 1992): 331–38. http://dx.doi.org/10.1017/s0022029900030600.

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SummaryThe three aspartic acid residues that form part of the Ca-binding site of mares' milk lysozyme have apparent pK values of 4·9, 4·3 and 4·1. The fluorescence of tryptophan has been used to compare the denaturation of mares' milk lysozyme by guanidinium chloride at various concentrations of Ca with that of hens' egg-white lysozyme (EC 3.2.1.17) and α-lactalbumin. Fluorescence revealed an intermediate stage in the denaturation of mares' milk lysozyme. The Ca-free form of mares' milk lysozyme is slightly more stable than that of α-lactalbumin, but its interaction with Ca is similar to that of α-lactalbumin, since only the native state binds Ca. Three-state models of denaturation can usefully be displayed on a ternary diagram.
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7

Dong, X. Y., J. H. Shi, and Y. Sun. "Cooperative Effect of Artificial Chaperones and Guanidinium Chloride on Lysozyme Renaturation at High Concentrations." Biotechnology Progress 18, no. 3 (June 7, 2002): 663–65. http://dx.doi.org/10.1021/bp0200191.

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8

Biswas, Biswajit, Aswathy N. Muttathukattil, Govardhan Reddy, and Prashant Chandra Singh. "Contrasting Effects of Guanidinium Chloride and Urea on the Activity and Unfolding of Lysozyme." ACS Omega 3, no. 10 (October 25, 2018): 14119–26. http://dx.doi.org/10.1021/acsomega.8b01911.

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9

Liu, Wei, Troy Cellmer, David Keerl, John M. Prausnitz, and Harvey W. Blanch. "Interactions of lysozyme in guanidinium chloride solutions from static and dynamic light-scattering measurements." Biotechnology and Bioengineering 90, no. 4 (2005): 482–90. http://dx.doi.org/10.1002/bit.20442.

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10

Chitra, Rajappa, and Paul E. Smith. "Molecular Association in Solution: A Kirkwood−Buff Analysis of Sodium Chloride, Ammonium Sulfate, Guanidinium Chloride, Urea, and 2,2,2-Trifluoroethanol in Water." Journal of Physical Chemistry B 106, no. 6 (February 2002): 1491–500. http://dx.doi.org/10.1021/jp011462h.

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11

Perriman, Adam W., Mark J. Henderson, Christian R. Evenhuis, Duncan J. McGillivray, and John W. White. "Effect of the Air−Water Interface on the Structure of Lysozyme in the Presence of Guanidinium Chloride." Journal of Physical Chemistry B 112, no. 31 (August 2008): 9532–39. http://dx.doi.org/10.1021/jp800354r.

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12

Mande, Shekhar C., and M. Elizabeth Sobhia. "Structural characterization of protein–denaturant interactions: crystal structures of hen egg-white lysozyme in complex with DMSO and guanidinium chloride." Protein Engineering, Design and Selection 13, no. 2 (February 2000): 133–41. http://dx.doi.org/10.1093/protein/13.2.133.

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13

WICKSTRÖM, Claes, Cecilia CHRISTERSSON, Julia R. DAVIES, and Ingemar CARLSTEDT. "Macromolecular organization of saliva: identification of ‘insoluble’ MUC5B assemblies and non-mucin proteins in the gel phase." Biochemical Journal 351, no. 2 (October 10, 2000): 421–28. http://dx.doi.org/10.1042/bj3510421.

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Stimulated human submandibular/sublingual (HSMSL) and whole saliva were separated into sol and gel phases and mucins were isolated by density-gradient centrifugation in CsCl/4M guanidinium chloride. MUC5B and MUC7 were identified using anti-peptide antisera raised against sequences within the MUC5B and MUC7 apoproteins respectively. MUC7 was found mainly in the sol phase of both HSMSL and whole saliva, but some MUC7 was consistently present in the gel phase, suggesting that this mucin may interact with the salivary gel matrix. In HSMSL saliva, MUC5B was found in the gel phase; however, most of the material was ‘insoluble’in guanidinium chloride and was only brought into solution by reduction. In whole saliva, the MUC5B mucin was present both in the sol and gel phases although some material was again ‘insoluble’. Rate-zonal centrifugation of whole saliva showed that MUC5B mucins in the sol phase were smaller than those in the gel phase, suggesting differences in oligomerization and/or degradation. Antibodies against IgA, secretory component, lysozyme and lactoferrin were used to study the distribution of non-gel-forming proteins in the different phases of saliva. The majority of these proteins was found in the sol phase of both HSMSL and whole saliva. However, a significant fraction was present in the gel phase of whole saliva, suggesting a post-secretory interaction with the salivary gel matrix. A monoclonal antibody against a parotid salivary agglutinin was used to show that this protein is present mainly in the gel phase of both whole saliva and parotid secretion.
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14

Sasahara, Kenji, Masao Sakurai, and Katsutoshi Nitta. "The volume and compressibility changes of lysozyme associated with guanidinium chloride and pressure-assisted unfolding 1 1Edited by P. E. Wright." Journal of Molecular Biology 291, no. 3 (August 1999): 693–701. http://dx.doi.org/10.1006/jmbi.1999.2982.

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15

Biswas, Biswajit, and Prashant Chandra Singh. "Molecular level insight into the counteraction of trehalose on the activity as well as denaturation of lysozyme induced by guanidinium chloride." Chemical Physics 527 (November 2019): 110489. http://dx.doi.org/10.1016/j.chemphys.2019.110489.

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16

Tsiganos, C. P., D. H. Vynios, and D. L. Kalpaxis. "Rooster comb hyaluronate—protein, a non-covalently linked complex." Biochemical Journal 235, no. 1 (April 1, 1986): 117–23. http://dx.doi.org/10.1042/bj2350117.

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Hyaluronate from rooster comb was isolated by ion-exchange chromatography on DEAE-cellulose from tissue extracts and papain digests. The preparations were labelled with [14C]acetic anhydride and subjected to CsCl-density-gradient centrifugation in 4 M-guanidinium chloride in the presence and absence of 4% ZwittergentTM 3-12. A radioactive protein fraction was separated from the hyaluronate when the zwitterionic detergent was also present. The protein could also be separated from the glycosaminoglycan by chromatography on Sepharose CL-6B eluted with the same solvent mixture. The protein fraction contained three protein bands of Mr 15,000-17,000 as assessed by polyacrylamide-gel electrophoresis in 0.1% SDS, and seemed to lack lysozyme activity. No evidence of other protein or amino acid(s) covalently linked with the hyaluronate was obtained. The hyaluronate-protein complex may be re-formed upon mixing the components, the extent of its formation depending on the conditions used. The results show that, as in chondrosarcoma [Mason, d'Arville, Kimura & Hascall (1982) Biochem. J. 207, 445-457] and teratocarcinoma cells [Prehm (1983) Biochem. J. 211, 191-198] the rooster comb hyaluronate also is not linked covalently to a core protein.
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17

Wallis, M., D. J. Gwilliam, and O. C. Wallis. "Preparation and characterization of a recombinant DNA-derived ovine growth hormone variant internally labelled with sulphur-35." Journal of Molecular Endocrinology 11, no. 3 (December 1993): 351–59. http://dx.doi.org/10.1677/jme.0.0110351.

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ABSTRACT 125I-Labelled polypeptide hormones have been extremely valuable for radioimmunoassays, receptor-binding studies and investigation of the processing and metabolism of hormones. However, such externally labelled material has the disadvantage that addition of one or more iodine atoms may alter the properties of the polypeptide. Furthermore, for studies on hormone metabolism and processing, the label may become separated from the hormone or its main breakdown products. Use of internally labelled polypeptides produced by biosynthesis can avoid such problems, but previously such material has usually been of low specific radioactivity, and unsuitable for many purposes. Here we describe the development of a procedure for the production of an internally labelled ovine GH analogue (oGH1) using a plasmid produced by recombinant DNA methods and expression in Escherichia coli. Bacteria were grown in medium containing a low sulphate concentration, and then incubated in medium containing 35SO42− as the sole sulphur source. Under these conditions, the bacteria incorporated 35S into proteins including GH. Purification of such material required considerable modification of previously described methods, because of the need to handle very small amounts of highly radioactive material. The bacteria were lysed using lysozyme, and inclusion bodies were solubilized using 6 m guanidinium chloride. [35S]oGH1 was renatured and then purified by gel filtration on Sephacryl S-100, followed by immunoaffinity chromatography and a second gel filtration step. Material prepared in this way had a specific radioactivity of 6–27 μCi/μg, and showed high 'bind-ability' to polyclonal and monoclonal antibodies and to receptors. 35S-Labelled material bound to receptors more effectively than 125I-labelled GH and showed improved stability. Such material appears to be well suited to receptor-binding studies and studies on the processing and metabolism of GH. The procedure developed should be applicable to other polypeptide hormones.
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