Results 291 to 300 of about 282,766 (336)

Staphylokinase as a Plasminogen Activator Component in Recombinant Fusion Proteins

Applied and Environmental Microbiology, 1999
ABSTRACT The plasminogen activator staphylokinase (SAK) is a promising thrombolytic agent for treatment of myocardial infarction. It can specifically stimulate the thrombolysis of both erythrocyte-rich and platelet-rich clots.
Steven Szarka, Hamid R. Habibi, E. G. Sihota, Sui-Lam Wong   +3 more
openaire   +3 more sources

Thrombolytic and anticoagulant effects of a recombinant staphylokinase-hirudin fusion protein

Thrombosis Research, 2021
A 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, Fan Zhang, Keyun Ren, Hao Gong, Chutse Wu, Yubin Liu, Junjie Huang, Kun He, Aiping Yu, Lvming Tian   +9 more
openaire   +3 more sources

Purification of recombinant proteins by fusion with thermally-responsive polypeptides

Nature Biotechnology, 1999
Elastin-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
openaire   +3 more sources

Cytotoxic Activity of Recombinant bFGF–rViscumin Fusion Proteins

Biochemical and Biophysical Research Communications, 2000
A 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, Jürgen Eck, Marc Gauert, Martin Langer, Arno Schmidt, Holger Zinke   +5 more
openaire   +3 more sources

Expression and Purification of Recombinant Proteins by Fusion to Maltose-Binding Protein

Molecular Biotechnology, 2000
The 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 ...
openaire   +2 more sources

Preparation of Recombinant RNase Single-Chain Antibody Fusion Proteins

Molecular Biotechnology, 2002
This 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
openaire   +5 more sources

Production of recombinant proteins in Escherichia coli tagged with the fusion protein CusF3H+

Protein Expression and Purification, 2017
Recombinant 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, Isaías Balderas-Rentería, Jose Ruben Morones-Ramirez, Teresa Vargas-Cortez   +3 more
openaire   +2 more sources

Recombinant Human Hb‐SOD Fusion Proteins

2013
Hemoglobin (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, Leif Bülow, Marie Grey   +2 more
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Construction and expression of recombinant fusion protein of thioredoxin-ApoO.

Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences, 2011
To construct human apolipoprotein O (apolipoprotein O, ApoO) expression vector and obtain recombinant fusion protein thioredoxin (Trx)-ApoO by pET prokaryotic expression system.The ApoO gene fragment from the human liver cDNA library was amplified by PCR. The resulting product was cloned into pET-32a(+) vector and sequenced.
Bi-lian Yu, Chen-Lu Wu, Shuiping Zhao, Dan Xiong   +3 more
openaire   +3 more sources

Self-cleaving fusion tags for recombinant protein production

Biotechnology Letters, 2011
Fusion expression is a common practice for recombinant protein production. Some fusion tags confer solubility on the target protein whereas others provide affinity handles that facilitate purification. However, the tag usually needs to be removed from the final product, which involves using expensive proteases or hazardous chemicals and requires ...
openaire   +3 more sources