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Open AccessJournal ArticleDOI

Potent Antithrombin Activity and Delayed Clearance From the Circulation Characterize Recombinant Hirudin Genetically Fused to Albumin

Summer Syed, +3 more
- 01 May 1997 - 
- Vol. 89, Iss: 9, pp 3243-3252
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TLDR
The results provide a rationale for future testing of the biological effects of HLA, and support the initial hypothesis that gene fusion of hirudin to albumin would result in the expression of a slowly cleared hirUDin molecule, as well as retention of high-affinity inhibition of thrombin by the fusion protein.
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This article is published in Blood.The article was published on 1997-05-01 and is currently open access. It has received 142 citations till now. The article focuses on the topics: Hirudin & Serum albumin.

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Citations
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Journal ArticleDOI

Effect of pegylation on pharmaceuticals

TL;DR: How PEGylation can result in drugs that are often more effective and safer, and which show improved patient convenience and compliance are reviewed.
Journal ArticleDOI

Chemistry for peptide and protein PEGylation.

TL;DR: PEG chemistry and methods of preparation are reviewed with a particular focus on new (second-generation) PEG derivatives, reversible conjugation and PEG structures.
Journal ArticleDOI

Albumin Binding as a General Strategy for Improving the Pharmacokinetics of Proteins

TL;DR: A series of peptides having the core sequence DICLPRWGCLW that specifically bind serum albumin from multiple species with high affinity are identified, suggesting a novel and generic method for improving the pharmacokinetic properties of rapidly cleared proteins.
Journal ArticleDOI

Pharmaceutical Strategies Utilizing Recombinant Human Serum Albumin

TL;DR: Gene manipulation techniques open up the possibility of making recombinant human serum albumin (rHSA) or mutants with desirable therapeutic properties and for protein fusion products, as well as site-directed mutants of HSA can be tailor made depending on the application required.
Journal ArticleDOI

Advances in PEGylation of important biotech molecules: delivery aspects

TL;DR: This review will discuss recent achievements in PEGylation processes with an emphasis on novel PEG-drugs constructs, the unrealized potential of P EGylation for non-injected routes of delivery, and also on PEGYLated versions of polymeric nanoparticles, including dendrimers and liposomes.
References
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Journal ArticleDOI

Unidirectional digestion with exonuclease III creates targeted breakpoints for DNA sequencing.

TL;DR: A method is described for the rapid generation and cloning of deletion derivatives well-suited for the sequencing of long stretches of DNA based on two useful features of exonuclease III: processive digestion at a very uniform rate and failure to initiate digestion at DNA ends with four-base 3'-protrusions.
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Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli.

TL;DR: A biosynthetic antibody binding site, which incorporated the variable domains of anti-digoxin monoclonal antibody 26-10 in a single polypeptide chain, was produced in Escherichia coli by protein engineering.
Journal Article

A comparison of recombinant Hirudin with Heparin for the treatment of acute coronary syndromes. The Global Use of Strategies to Open Occluded Coronary Arteries (GUSTO) IIb Investigators

TL;DR: Recombinant hirudin provided a small advantage, as compared with heparin, principally related to a reduction in the risk of nonfatal myocardial infarction and was not associated with a greater risk of major bleeding complications.
Journal ArticleDOI

The structure of a complex of recombinant hirudin and human alpha-thrombin

TL;DR: The crystallographic structure of a recombinant hirudin-thrombin complex has been solved at 2.3 angstrom (A) resolution and abundant interactions may account for the high affinity and specificity of hirUDin.
Journal ArticleDOI

A versatile in vivo and in vitro eukaryotic expression vector for protein engineering

TL;DR: The pSG5 vector as mentioned in this paper was constructed by combining the eukaryotic expression vector, pKCR2, and the high copy plasmid vector Bluescribe Ml3+ (Stratagene).
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