Keyword Search
Free Journal Login
Login    Register   

Login to your account

No Account Yet? Fields marked with an asterisk (*) are required.

Please enter a valid Username. No spaces, at least 2 characters and must contain only letters and numbers.
Please enter a valid Password. No spaces, at least 4 characters and must contain only letters and numbers.
Passwords do not match.
Please enter a valid e-mail address.
E-mails do not match. ?>

Journal on iPad

Call for Articles

There is no fee to publish with us.

PLEASE READ BEFORE PROCEEDING: By purchasing an article in PDF format, you are agreeing to follow our Article Policy. Use the "Buy Now" button to purchase an article.  Once checkout is complete, a download link will be sent to the email address that you provide during checkout.


Use the KEYWORD search option located in the top left column to search for keywords, names, and phrases. If you still can't find what you're looking for, please This e-mail address is being protected from spambots. You need JavaScript enabled to view it .

Initial Clarification by Aqueous Two-Phase Partitioning of Leaf Extracts from Solanum tuberosum Plants Expressing Recombinant Therapeutic Proteins

by Keith D. Miller, PhD, Johnway Gao, PhD, Brian S. Hooker, PhD
Volume 3, Issue 2 (March/April 2004)

The use of plants as protein expression hosts for human therapeutic proteins is emerging as a safe and cost-effective alternative to microbial and mammalian cell culture. Pharmaceutical protein production is typically carried out in microbes and mammalian cell culture because of their high production potential and/or ability to produce complex eukaryotic proteins. However, immense costs are typically required for production facilities to support their growth. To offset these costs, companies usually build and expand a production facility over several years. In fact, it has been predicted that the demand for high-value pharmaceuticals produced by cell culture will quickly surpass the ability of pharmaceutical companies to produce them...

Miller KD, Gao J, Hooker BS. Initial Clarification by Aqueous Two-Phase Partitioning of Leaf Extracts from Solanum tuberosum Plants Expressing Recombinant Therapeutic Proteins. BioProcess J, 2004; 3(2): 47-51.

Encapsulating Cells for High-Productivity Recombinant Protein Expression

by Christoph Heinzen, PhD, Andreas Berger, PhD, and Ian Marison, PhD
Volume 3, Issue 2 (March/April 2004)

The first use of mammalian cell culture for the production of vaccines dates back to polio vaccine development in the 1950s. The development of hybridoma technology in the 1970s further stimulated the use of mammalian cells for the production of monoclonal antibodies. Together with developments in genetic engineering, it therefore became possible to produce a wide range of recombinant proteins as well as to improve cell metabolism. Animal cells are now widely used in industrial processes to obtain complex glycoproteins with correct posttranslational modifications and biological activity for diagnostic and therapeutic applications. Animal cells are the main source for commercially available recombinant proteins such as tissue plasminogen activator (tPa), erythropoietin (EPO), DNAse, factor VIII, interferon-ß, and monoclonal antibodies...

Heinzen C, Berger A, Marison I. Encapsulating Cells for High-Productivity Recombinant Protein Expression. BioProcess J, 2004; 3(2): 53-56.

Positioning a Blood Center to Grasp Biotech Opportunities

by Edward P. Scott, MD
Volume 3, Issue 2 (March/April 2004)

The modern age of blood transfusion began after the Second World War, as detailed in Douglas Starr’s book, Blood: An Epic History of Medicine and Commerce. During the war, it became apparent that early and aggressive medical treatment utilizing whole blood or plasma could increase the chances of survival for military personnel wounded in combat. In the United States, a national program to encourage blood donation was created to provide the needed blood, which was then shipped as whole blood or plasma to war zones. After the war, physicians were eager to apply surgical advances developed on and off the battlefield to the care of the general population. Because these advances relied on blood transfusion, for the public to realize their benefit, adequate supplies of whole blood and blood components needed to be available to hospitals across the country. This was often not the case...

Scott EP. Positioning a Blood Center to Grasp Biotech Opportunities. BioProcess J, 2004; 3(2): 59-63.

Molecular Engineering of “Pathotropic” Targeting for Cancer Gene Therapy

by Jennifer Noe Pahre, JD, Michael Fuchs, JD, John P. Levy, Erlinda M. Gordon, MD, and Frederick L. Hall, PhD
Volume 3, Issue 1 (January/February 2004)

More than 70 percent of all prospective gene transfer/gene therapy protocols are designed to treat metastatic cancer. A large number of such protocols involve strategies to attempt cancer immunization via cell-based gene transfer of cytokines or tumor antigens, while others involve the delivery of oncolytic viruses or vectors bearing prodrugs, chemoprotective agents, antisense constructs, or tumor suppressor genes. However, a major unresolved problem that has impeded the progress of cancer gene therapy to the clinic is that of inefficient gene delivery to target cells in vivo. In this regard, the advent of pathotropic targeting launches a new paradigm in cancer gene therapy. By targeting the histopathology of the cancerous lesion — rather than the cancer cells per se — to effectively concentrate the gene vector within primary and metastatic tumors, the safety and efficacy of intravenously administered vector nanoparticles were increased significantly in animal models of cancer. This article describes the development of the pathotropic Targeted Delivery System (TDS) that now serves as the guidance system for “smart” nanoparticles bearing designer killer genes for cancer gene therapy...

Noe Pahre J, Fuchs M, Levy JP, Gordon EM, Hall FL. Molecular Engineering of “Pathotropic” Targeting for Cancer Gene Therapy.
BioProcess J, 2004; 3(1): 21-26.

Optimisation of Virus Stock Production and Cell Infection Conditions for Protein Expression

by Loïc Glez, Christophe Losberger, and Thierry Battle, PhD
Volume 3, Issue 1 (January/February 2004)

Variation of viral titre and recombinant product yields reported for the baculovirus expression vector system have been attributed to many specific infection variables. These include multiplicity of infection (MOI) and cell density at time of infection and time of harvest, as well as virus bank quality and efficiency. The MOI is defined as the number of plaque forming units (pfu) per cell that are added at the time of infection. Virus titre (pfu/ml) is determined by the plaque assay method. The MOI parameter is easily manipulated and may be important in optimising recombinant protein yields. Other sources of variation during both cell growth and viral infection phases may be responsible for the range of reported yields. Past studies in our laboratory compared the behaviour of cells infected with high and low MOI values, specifically regarding nutrient limitation and deprivation. In addition to these aspects, the quality of the virus bank may be an important factor which influences heterologous protein yields in the insect cell baculovirus system. Thus, production yields may be correlated to virus efficiency...

Glez L, Losberger C, Battle T. Optimisation of Virus Stock Production and Cell Infection Conditions for Protein Expression.
BioProcess J, 2004; 3(1): 27-32.

Development of a Parvovirus Assay Using rNS-1 His-tagged Antigen

by Elena M. Seletskaia, J. Paul Cowley, Michelle L. Wunderlich, Steven M. Jennings, Kenneth S. Henderson, PhD, William R. Shek, PhD, and Rajeev K. Dhawan, PhD
Volume 3, Issue 1 (January/February 2004)

Parvoviruses are one of the most prevalent infectious agents in the laboratory rodent. Their effect on research can range from immune dysfunction that may mislead researchers when interpreting results to lethal effects on animals. Until recently parvovirus infection in mice was thought to be caused by minute mouse virus (MMV) and in rats by rat viral agents in the KRV or H-1 serogroups. Relatively newly discovered viruses in these groups are mouse (MPV) and rat parvoviruses (RPV-1 and 2). Parvoviruses are 15–20 nm in diameter and are single-stranded DNA viruses of about 5,000 nucleotides, which replicate through a double-stranded DNA intermediate. The protein composition consists of three structural or capsid proteins providing the viral coat (VP-1, VP-2, and VP-3) and two non-structural proteins involved in viral replication (NS-1 and NS-2). Among the capsid proteins,VP-2 is the major protein...

Seletskaia EM, Cowley JP, Wunderlich ML, Jennings SM, Henderson KS, Shek WR, Dhawan RK. Development of a Parvovirus Assay Using rNS-1 His-tagged Antigen.
BioProcess J, 2004; 3(1): 35-39.

<< Start < Prev 41 42 43 44 45 46 47 48 49 50 Next > End >>

Website Sponsors
Endorsed Events
Please update your Flash Player to view content.
Please update your Flash Player to view content.