Results 191 to 200 of about 577,747 (248)
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Purification of recombinant proteins by fusion with thermally-responsive polypeptides
Nature Biotechnology, 1999Elastin-like polypeptides (ELPs) undergo a reversible, inverse phase transition. Below their transition temperature (Tt), ELPs are soluble in water, but when the temperature is raised above Tt, phase transition occurs, leading to aggregation of the polypeptide. We demonstrate a method for purification of soluble fusion proteins incorporating an ELP tag.
Dan E. Meyer, Ashutosh Chilkoti
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Thrombolytic and anticoagulant effects of a recombinant staphylokinase-hirudin fusion protein
Thrombosis Research, 2021A pure recombinant staphylokinase-hirudin fusion protein (SFH) was obtained by recombinant genetic engineering and purification techniques. The thrombolytic and anticoagulant activities of SFH were investigated using in vitro coagulation models and chromogenic assays.
Qiaoyan Dong +9 more
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Cytotoxic Activity of Recombinant bFGF–rViscumin Fusion Proteins
Biochemical and Biophysical Research Communications, 2000A fusion protein (bFGF-rMLA), containing the mitogen basic fibroblast growth factor (bFGF) and the cytotoxic component of rViscumin (recombinant mistletoe lectin), the enzymatic A-chain (rMLA), was expressed in Escherichia coli, purified, and functionally characterized.
Babette Möckel +5 more
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Biochemistry, 1996
Aquaporin-1 (AQP1) is a member of a family of integral membrane proteins, the aquaporins, which function as molecular channels for the movement of water across the plasma membrane. While the primary structure of AQP1 has been obtained from the cloning of
W. Stamer, R. Snyder, J. Regan
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Aquaporin-1 (AQP1) is a member of a family of integral membrane proteins, the aquaporins, which function as molecular channels for the movement of water across the plasma membrane. While the primary structure of AQP1 has been obtained from the cloning of
W. Stamer, R. Snyder, J. Regan
semanticscholar +1 more source
Journal of Agricultural and Food Chemistry, 2002
A method was developed for the production of a hydrolyzed/polymerized whey protein derivative with altered solution and gelation properties using a combination of recombinant DNA and immobilized enzyme technologies.
C. Wilcox +3 more
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A method was developed for the production of a hydrolyzed/polymerized whey protein derivative with altered solution and gelation properties using a combination of recombinant DNA and immobilized enzyme technologies.
C. Wilcox +3 more
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Expression and Purification of Recombinant Proteins by Fusion to Maltose-Binding Protein
Molecular Biotechnology, 2000The pMAL vectors provide a method for purifying proteins from cloned genes by fusing them to maltose-binding protein (MBP, product of malE), which binds to amylose. The vectors use the tac promoter and the translation initiation signals of MBP to give high-level expression of the fusion, and an affinity purification for MBP to isolate the fusion ...
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Preparation of Recombinant RNase Single-Chain Antibody Fusion Proteins
Molecular Biotechnology, 2002This article describes the construction, expression, and purification of RNase single-chain antibody fusion proteins. To construct a fusion protein, the gene for each moiety, the RNase and the binding ligand, is modified separately to contain complementary DNA encoding a 13 amino acid spacer that separates the RNase from the binding moiety. Appropriate
Susanna M. Rybak, Dianne L. Newton
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Protein Expression and Purification, 1998
We report the biotechnical production of peptides of approximately 35-50 amino acids in length containing one intramolecular disulfide bridge, using a recombinant fusion tail approach.
H. Döbeli +7 more
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We report the biotechnical production of peptides of approximately 35-50 amino acids in length containing one intramolecular disulfide bridge, using a recombinant fusion tail approach.
H. Döbeli +7 more
semanticscholar +1 more source
Production of recombinant proteins in Escherichia coli tagged with the fusion protein CusF3H+
Protein Expression and Purification, 2017Recombinant protein expression in the bacterium Escherichia coli still is the number one choice for large-scale protein production. Nevertheless, many complications can arise using this microorganism, such as low yields, the formation of inclusion bodies, and the requirement for difficult purification steps.
Xristo Zarate +3 more
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Recombinant Human Hb‐SOD Fusion Proteins
2013Hemoglobin (Hb) can produce reactive oxygen species, including superoxide anions, which are intrinsically toxic. Superoxide dismutase (SOD) is present in red blood cells (RBCs) and provides important protection against such oxidative stress. Upon hemolysis, Hb becomes released from the RBCs and the normal protection systems involving SOD and catalase ...
Khuanpiroon Ratanasopa +2 more
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