Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli

1989 ◽  
Vol 210 (1) ◽  
pp. 79-89 ◽  
Author(s):  
Chaitan Khosla ◽  
James E. Bailey
Keyword(s):  
Escherichia Coli ◽  
Vitreoscilla Hemoglobin ◽  
Periplasmic Space

Expression of Double Vitreoscilla Hemoglobin Enhances Growth and Alters Ribosome and tRNA Levels in Escherichia coli

2002 ◽  
Vol 18 (3) ◽  
pp. 652-656 ◽  
Author(s):  
V. Roos ◽  
C.I.J. Andersson ◽  
C. Arfvidsson ◽  
K.-G. Wahlund ◽  
L. Bulow
Keyword(s):  
Escherichia Coli ◽  
Vitreoscilla Hemoglobin

scholarly journals Type 3-specific synthase of Streptococcus pneumoniae (Cap3B) directs type 3 polysaccharide biosynthesis in Escherichia coli and in pneumococcal strains of different serotypes.

1996 ◽  
Vol 184 (2) ◽  
pp. 449-455 ◽  
Author(s):  
C Arrecubieta ◽  
R López ◽  
E García
Keyword(s):  
Escherichia Coli ◽  
Streptococcus Pneumoniae ◽  
High Molecular Mass ◽  
Cell Fractionation ◽  
Periplasmic Space ◽  
Polysaccharide Biosynthesis ◽  
E Coli ◽  
Escherichia Coli Cells ◽  
Immunological Tests ◽  
Type 3

The cap3B gene, which is involved in the formation of the capsule of Streptococcus pneumoniae type 3, encodes a 49-kD protein that has been identified as a polysaccharide synthase. Escherichia coli cells harboring the recombinant plasmid pTBP3 (cap3B) produced pneumococcal type 3 polysaccharide, as demonstrated by immunological tests. Biochemical and cell fractionation analyses revealed that this polysaccharide had a high molecular mass and was localized in substantial amounts in the periplasmic space of E. coli. Unencapsulated (S-2), laboratory pneumococcal strains synthesized type 3 polysaccharide by transformation with plasmid pLSE3B harboring cap3B. In addition, encapsulated pneumococci of types 1, 2, 5, or 8 transformed with pLSE3B can direct the synthesis of pneumococcal type 3 polysaccharide, leading to the formation of strains that display binary type of capsule.

scholarly journals Protein A-Mouse Acidic Mammalian Chitinase-V5-His Expressed in Periplasmic Space of Escherichia coli Possesses Chitinase Functions Comparable to CHO-Expressed Protein

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e78669 ◽  
Author(s):  
Akinori Kashimura ◽  
Kazuaki Okawa ◽  
Kotarou Ishikawa ◽  
Yuta Kida ◽  
Kokoro Iwabuchi ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein A ◽  
Periplasmic Space ◽  
Acidic Mammalian Chitinase
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