Process Development for the Large Scale Production of Clinical Grade Human Monoclonal Antibody Using a Cytopilot Fluidized Bed Reactor

1997 ◽  
pp. 447-450 ◽  
Author(s):  
G. Klima ◽  
G. Kreismayr ◽  
D. Müller ◽  
C. Schmatz ◽  
S. Wiederkum ◽  
...  
2002 ◽  
Vol 364 (5-6) ◽  
pp. 568-572 ◽  
Author(s):  
Yao Wang ◽  
Fei Wei ◽  
Guohua Luo ◽  
Hao Yu ◽  
Guangsheng Gu

Catalysts ◽  
2019 ◽  
Vol 9 (5) ◽  
pp. 433 ◽  
Author(s):  
Si-si Xie ◽  
Lingyun Zhu ◽  
Xin-yuan Qiu ◽  
Chu-shu Zhu ◽  
Lv-yun Zhu

Monoterpenes are commonly applied as pharmaceuticals and valuable chemicals in various areas. The bioproduction of valuable monoterpenes in prokaryotic microbial hosts, such as E. coli, has progressed considerably thanks to the development of different outstanding approaches. However, the large-scale production of monoterpenes still presents considerable limitations. Thus, process development warrants further investigations. This review discusses the endogenous methylerythritol-4-phosphate-dependent pathway engineering and the exogenous mevalonate-dependent isoprenoid pathway introduction, as well as the accompanied optimization of rate-limiting enzymes, metabolic flux, and product toxicity tolerance. We suggest further studies to focus on the development of systematical, integrational, and synthetic biological strategies in light of the inter disciplines at the cutting edge. Our review provides insights into the current advances of monoterpene bioengineering and serves as a reference for future studies to promote the industrial production of valuable monoterpenes.


Blood ◽  
1982 ◽  
Vol 59 (3) ◽  
pp. 664-670 ◽  
Author(s):  
AH Goodall ◽  
G Kemble ◽  
DP O'Brien ◽  
E Rawlings ◽  
F Rotblat ◽  
...  

Abstract A murine hybridoma clone is described that grows continuously in culture and produces a monoclonal antibody we have called Royal Free Monoclonal Antibody to factor IX No. 1 (RFF-IX/1). This has high affinity for a coagulation site on factor IX. RFF-IX/1 immobilised on sepharose can be used to deplete factor IX from normal human plasma. This immunoaffinity depleted plasma is indistinguishable from severe Christmas disease plasma and can be used as the substrate in a one stage coagulation assay for factor IX. The affinity column has high capacity and can be regenerated so that large scale production from normal plasma of factor IX deficient plasma as a diagnostic reagent is now feasible.


Blood ◽  
1982 ◽  
Vol 59 (3) ◽  
pp. 664-670
Author(s):  
AH Goodall ◽  
G Kemble ◽  
DP O'Brien ◽  
E Rawlings ◽  
F Rotblat ◽  
...  

A murine hybridoma clone is described that grows continuously in culture and produces a monoclonal antibody we have called Royal Free Monoclonal Antibody to factor IX No. 1 (RFF-IX/1). This has high affinity for a coagulation site on factor IX. RFF-IX/1 immobilised on sepharose can be used to deplete factor IX from normal human plasma. This immunoaffinity depleted plasma is indistinguishable from severe Christmas disease plasma and can be used as the substrate in a one stage coagulation assay for factor IX. The affinity column has high capacity and can be regenerated so that large scale production from normal plasma of factor IX deficient plasma as a diagnostic reagent is now feasible.


2016 ◽  
Vol 24 ◽  
pp. S279-S280
Author(s):  
Alexandre Audy ◽  
Marc-André Robert ◽  
Parminder Chahal ◽  
Rénald Gilbert ◽  
Bruno Gaillet

2007 ◽  
Vol 24 (2) ◽  
pp. 347-349 ◽  
Author(s):  
Jaehyeon Park ◽  
Dal Hee Bae ◽  
Seung Yong Lee ◽  
Jini Kwak ◽  
Hai Woong Park ◽  
...  

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