The solubility and fractionation of β1-lactoglobulin

Tombs, M. P.

doi:10.1042/bj0670517

Cited by 26 publications

(5 citation statements)

References 10 publications

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“…PEG [25] and glycerol [26] were added to increase the viscosity of the system and thus help prevent aggregation. ␤-Mercaptoethanol was used as reducing agent to prevent the oxidation reaction of thiol group of cysteine which is prone to denature the enzyme activity [27]. BSA was assayed since it was reported useful in preservation of protein [28].…”

Section: Discussionmentioning

confidence: 99%

Effect of CaCl2 as activity stabilizer on purification of heparinase I from Flavobacterium heparinum

Wang

et al. 2006

Journal of Chromatography B

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Section: Discussionmentioning

confidence: 99%

Effect of CaCl2 as activity stabilizer on purification of heparinase I from Flavobacterium heparinum

Wang

et al. 2006

Journal of Chromatography B

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“…Protein denaturation is commonly defined as any noncovalent change in the structure of a protein [10]. This structural modification affects the secondary, tertiary, or quaternary structure of the molecules.…”

Section: Denaturationmentioning

confidence: 99%

“…This structural modification affects the secondary, tertiary, or quaternary structure of the molecules. For enzymes, denaturation can be defined as the loss of enough structure rendering the enzyme inactive [10].…”

Section: Denaturationmentioning

confidence: 99%

The Importance of Sample Handling in Neuropeptidomics

et al. 2007

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“…One limitation to the clinical use of most therapeutic proteins is their short half‐lives as a result of inactivation in vivo . The most common form of inactivation in vivo is enzymic modification, particularly enzymic proteolysis [1]. Protecting medically important proteins from proteolytic inactivation may be achieved by use of poly(ethene glycol) [2], albumin [3] and antibodies [4–6].…”

Section: Introductionmentioning

confidence: 99%

Selecting and expressing protective single‐chain Fv fragment to stabilize L‐asparaginase against inactivation by trypsin

Guo

Yan

Qian

et al. 2000

Biotech and App Biochem

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Four non-inhibitory specific single-chain Fv (sc Fv) fragments directed against L-asparaginase (ASNase) of Escherichia coli were selected from a synthetic phage-display scFv library. The scFv46 fragment could enhance the resistance of ASNase to trypsin proteolysis, with 70% of the initial ASNase activity present after the ASNase-scFv46 complex had been treated with trypsin for 30 min at 37 degrees C, whereas little residual activity was detected without the scFv46 fragment. The scFv46 gene was cloned to an expression vector pET-21a and expressed at high levels (about 45% of total cell protein) in E. coli BL21 (DE3) as inclusion bodies. The refolded and purified scFv46 fragment was proved to protect ASNase, and the protective effect was further confirmed by SDS/PAGE. It was found that under optimum conditions of molar ratio of scFv to ASNase, incubation time and temperature, the residual activity of the ASNase-scFv46 complex could reach about 78% after treatment with trypsin for 30 min at 37 degrees C. The results demonstrated that scFv fragments prepared by phage-antibody library technology could be used to protect target proteins.

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The solubility and fractionation of β1-lactoglobulin

Cited by 26 publications

References 10 publications

Effect of CaCl2 as activity stabilizer on purification of heparinase I from Flavobacterium heparinum

Effect of CaCl2 as activity stabilizer on purification of heparinase I from Flavobacterium heparinum

The Importance of Sample Handling in Neuropeptidomics

Selecting and expressing protective single‐chain Fv fragment to stabilize L‐asparaginase against inactivation by trypsin

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