Expression of Biologically Active Human SPARC inEscherichia coli

1996 ◽  
Vol 325 (1) ◽  
pp. 8-19 ◽  
Author(s):  
James A. Bassuk ◽  
François Baneyx ◽  
Robert B. Vernon ◽  
Sarah E. Funk ◽  
E.Helene Sage
Keyword(s):  
Biologically Active ◽  
Inescherichia Coli

scholarly journals The expression of biologically active cholera toxin inEscherichia coli

1982 ◽  
Vol 10 (16) ◽  
pp. 4883-4890 ◽  
Author(s):  
Maria L. Gennaro ◽  
Peter J. Greenaway ◽  
David A. Broadbent
Keyword(s):  
Cholera Toxin ◽  
Biologically Active ◽  
Inescherichia Coli

Efficient Secretion of Biologically Active Recombinant OB Protein (Leptin) inEscherichia coli,Purification from the Periplasm and Characterization

1998 ◽  
Vol 12 (2) ◽  
pp. 249-258 ◽  
Author(s):  
Yves Guisez ◽  
Ina Faché ◽  
L.Arthur Campfield ◽  
Françoise J. Smith ◽  
Adrienne Farid ◽  
...  
Keyword(s):  
Biologically Active ◽  
Inescherichia Coli ◽  
Ob Protein

scholarly journals Overproduction of Biologically-active Human Nerve Growth Factor inEscherichia coli

1992 ◽  
Vol 56 (12) ◽  
pp. 1985-1990 ◽  
Author(s):  
Kiyoshi Fujimori ◽  
Shinichi Fukuzono ◽  
Naoe Kotomura ◽  
Norihito Kuno ◽  
Norio Shimizu
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Biologically Active ◽  
Inescherichia Coli ◽  
Nerve Growth ◽  
Human Nerve

Expression of Biologically Active Isoforms of the Tumor Angiogenesis Factor VEGF inEscherichia coli

1996 ◽  
Vol 222 (2) ◽  
pp. 249-255 ◽  
Author(s):  
Gerhard Siemeister ◽  
Bernhard Schnurr ◽  
Katja Mohrs ◽  
Christoph Schächtele ◽  
Dieter Marmé ◽  
...  
Keyword(s):  
Tumor Angiogenesis ◽  
Biologically Active ◽  
Inescherichia Coli ◽  
Angiogenesis Factor

scholarly journals Production of biologically active light chain of tetanus toxin inEscherichia coli

FEBS Letters ◽  
1993 ◽  
Vol 323 (3) ◽  
pp. 218-222 ◽  
Author(s):  
Neil F. Fairweather ◽  
Dagmar Sanders ◽  
Debbie Slater ◽  
Martina Hudel ◽  
E. Habermann ◽  
...  
Keyword(s):  
Light Chain ◽  
Tetanus Toxin ◽  
Biologically Active ◽  
Inescherichia Coli

Cloning, High-Yield Expression inEscherichia coli,and Purification of Biologically Active HIV-1 Tat Protein

1996 ◽  
Vol 8 (1) ◽  
pp. 75-84 ◽  
Author(s):  
Thomas Kirsch ◽  
Markus Boehm ◽  
Oliver Schuckert ◽  
Armin U. Metzger ◽  
Dieter Willbold ◽  
...  
Keyword(s):  
Biologically Active ◽  
High Yield ◽  
Inescherichia Coli ◽  
Tat Protein ◽  
Expression Inescherichia Coli ◽  
Hiv 1

Characterization of photosystem II with the atomic-force microscope

1992 ◽  
Vol 50 (2) ◽  
pp. 1146-1147
Author(s):  
Kathleen M. Marr ◽  
Mary K. Lyon
Keyword(s):  
Photosystem Ii ◽  
Atomic Force Microscope ◽  
Three Dimensional ◽  
Biologically Active ◽  
Atomic Force ◽  
Freeze Etching ◽  
Image Averaging ◽  
Oxygen Evolving ◽  
Averaging Techniques

Photosystem II (PSII) is different from all other reaction centers in that it splits water to evolve oxygen and hydrogen ions. This unique ability to evolve oxygen is partly due to three oxygen evolving polypeptides (OEPs) associated with the PSII complex. Freeze etching on grana derived insideout membranes revealed that the OEPs contribute to the observed tetrameric nature of the PSIl particle; when the OEPs are removed, a distinct dimer emerges. Thus, the surface of the PSII complex changes dramatically upon removal of these polypeptides. The atomic force microscope (AFM) is ideal for examining surface topography. The instrument provides a topographical view of individual PSII complexes, giving relatively high resolution three-dimensional information without image averaging techniques. In addition, the use of a fluid cell allows a biologically active sample to be maintained under fully hydrated and physiologically buffered conditions. The OEPs associated with PSII may be sequentially removed, thereby changing the surface of the complex by one polypeptide at a time.

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