scholarly journals Identification, purification, and characterization of antigen-activated and antigen-specific human B lymphocytes.

1983 ◽  
Vol 157 (5) ◽  
pp. 1692-1697 ◽  
Author(s):  
J H Kehrl ◽  
A S Fauci

Activated pneumococcal polysaccharide (PPS)-specific human B lymphocytes have been purified and examined in vitro. They are large cells that are refractory to further activation by antigen, anti-Ig, or Staphylococcus aureus Cowan strain I, but they respond directly by proliferation to B cell growth factors. In addition, they express the isotype pattern of activated cells and a surface marker of activated lymphocytes called 4F2. Finally, they contain a subset of cells that spontaneously secrete PPS-specific antibody.

1988 ◽  
Vol 251 (2) ◽  
pp. 461-466 ◽  
Author(s):  
I Vidal ◽  
J González ◽  
A Bernardo ◽  
R Martín

A method was developed to purify diacetyl-reducing enzymes from Staphylococcus aureus. Two enzymes capable of catalysing diacetyl reduction were isolated, neither of which turned out to be a specific diacetyl reductase. One of them is a lactate dehydrogenase similar to the one from Staphylococcus epidermidis, which accepts diacetyl, although poorly. The other one uses as coenzyme beta-NAD and reduces uncharged alpha-dicarbonyls with more than three carbon atoms (especially the alpha-diketones diacetyl and pentane-2,3-dione), producing the L(+) form of the corresponding alpha-hydroxycarbonyls. This enzyme has an Mr of 68,000 and is, most probably, a monomer. Its optimum pH is 6.0. Its shows a high affinity for NADH and a rather low one for diacetyl, which, at least in vitro, does not seem to be as good a substrate as pentane-2,3-dione. We propose for it the systematic name L-alpha-hydroxyketone: NAD+ oxidoreductase and the recommended name of alpha-diketone reductase (NAD). We also suggest that the diacetyl reductase entry in the I.U.B. classification be suppressed.


1986 ◽  
Vol 261 (4) ◽  
pp. 1924-1928
Author(s):  
R Lobb ◽  
J Sasse ◽  
R Sullivan ◽  
Y Shing ◽  
P D'Amore ◽  
...  

2001 ◽  
Vol 18 (2) ◽  
pp. 107-112 ◽  
Author(s):  
Joaquim Ruiz ◽  
Josep M. Sierra ◽  
M.Teresa Jiménez De Anta ◽  
Jordi Vila

2013 ◽  
Vol 6 (1) ◽  
pp. 205-209
Author(s):  
Rathnakar Reddi KVN ◽  
Santhosh Kumar Pasupuleti ◽  
Venkateswara Prasad Uppu ◽  
Yeswanth Sthanikam ◽  
Swarupa Vimjam ◽  
...  

2007 ◽  
Vol 189 (24) ◽  
pp. 8871-8879 ◽  
Author(s):  
Zhibiao Fu ◽  
Niles P. Donegan ◽  
Guido Memmi ◽  
Ambrose L. Cheung

ABSTRACT The mazEF homologs of Staphylococcus aureus, designated mazEFsa , have been shown to cotranscribe with the sigB operon under stress conditions. In this study, we showed that MazEF Sa , as with their Escherichia coli counterparts, compose a toxin-antitoxin module wherein MazF Sa leads to rapid cell growth arrest and loss in viable CFU upon overexpression. MazF Sa is a novel sequence-specific endoribonuclease which cleaves mRNA to inhibit protein synthesis. Using ctpA mRNA as the model substrate both in vitro and in vivo, we demonstrated that MazF Sa cleaves single-strand RNA preferentially at the 5′ side of the first U or 3′ side of the second U residue within the consensus sequences VUUV′ (where V and V′ are A, C, or G and may or may not be identical). Binding studies confirmed that the antitoxin MazE Sa binds MazF Sa to form a complex to inhibit the endoribonuclease activity of MazF Sa . Contrary to the system in E. coli, exposure to selected antibiotics augmented mazEFsa transcription, akin to what one would anticipate from the environmental stress response of the sigB system. These data indicate that the mazEF system of S. aureus differs from the gram-negative counterparts with respect to mRNA cleavage specificity and antibiotic stresses.


1979 ◽  
Vol 57 (6) ◽  
pp. 945-958 ◽  
Author(s):  
Kostas Iatrou ◽  
Lashitew Gedamu ◽  
Gordon H. Dixon

Poly(A)+ protamine mRNA (pmRNA) components were isolated after separation on denaturing preparative polyacrylamide gels. The four size classes of protamine mRNA described previously were found to contain poly(A) tracts of different lengths. The pmRNA1 was found to be associated with (A)110, pmRNA2 with (A)90, pmRNA3 with (A)85, and pmRNA4 with (A)69. Following deadenylation with RNase H after duplex formation with oligo-dT, the isolated mRNAs were found to be still heterogeneous, although highly enriched in certain of the deadenylated components. DNA complementary to the isolated mRNAs (cDNA) was synthesized in vitro. Following depurination, the oligopyrimidine maps indicated that C7T4, corresponding to an Arg-Arg-Gly-Gly sequence in protamine and originally thought to be characteristic of all mRNA components, is present in only one or possibly two of the components. Cross-hybridizations between the cDNAs and the four poly(A)+ pmRNAs indicated that a basic polynucleotide unit of substantial length is common to all four mRNAs and that the existing nucleotide sequence variations probably originate from one or both of the non-coding portions of the mRNA molecules.


1997 ◽  
Vol 43 (6) ◽  
pp. 345-354 ◽  
Author(s):  
T. D. Nguyen ◽  
Melanie J. Smith ◽  
Peter Hersey

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