The role of the lysine binding sites of human plasminogen in the fibrinogen stimulated rate of active site formation in the streptokinase-plasminogen equimolar complex

1984 ◽  
Vol 34 (6) ◽  
pp. 499-506 ◽  
Author(s):  
James H. Smith ◽  
Joseph P. Morris ◽  
Bakshy A. Chibber ◽  
Francis J. Castellino
2001 ◽  
Vol 56 (9-10) ◽  
pp. 843-847
Author(s):  
Dessislava Nikolova Georgieva ◽  
Stanka Stoeva ◽  
Wolfgang Voelter ◽  
Nicolay Genov

Abstract The active site of Viviparus ater (mollusc) hemocyanin was investigated using the fact that the binding of dioxygen to the binuclear copper-containing sites of hemocyanins is connected with the appearance of specific dichroic bands which are very sensitive to changes in the structrure and polarity of the environment. Oxy-Viviparus ater hemocyanin exhibits near UV and visible circular dichroism spectra different from those of other molluscan and arthropo-dan hemocyanins. These differences are due probably to variations in the geometry or charge distribution in the dioxygen binding sites of the compared proteins.The thermostability of Viviparus ater hemocyanin and the significance of the copper-dioxy-gen system for the stability were also investigated. “Melting” temperatures, Tm, of 77 °C for the oxy-hemocyanin and 57 °C for the apo-protein were calculated from the denaturation curves which demonstrates the considerable role of the binuclear active site for the thermostability. Viviparus ater hemocyanin is more thermostable than other hemocyanins for which data are published.


PLoS ONE ◽  
2015 ◽  
Vol 10 (2) ◽  
pp. e0117836 ◽  
Author(s):  
Eun Hye Lee ◽  
Kitaik Lee ◽  
Kwang Yeon Hwang ◽  
Hwa-Young Kim

FEBS Journal ◽  
2010 ◽  
Vol 277 (21) ◽  
pp. 4549-4561 ◽  
Author(s):  
Wayne M. Patrick ◽  
Yoshio Nakatani ◽  
Susan M. Cutfield ◽  
Miriam L. Sharpe ◽  
Rochelle J. Ramsay ◽  
...  

2017 ◽  
Vol 5 (8) ◽  
pp. 4199-4206 ◽  
Author(s):  
Minhyoung Kim ◽  
Hee Soo Kim ◽  
Sung Jong Yoo ◽  
Won Cheol Yoo ◽  
Yung-Eun Sung

We investigated the carbon support microporosity effect on active site formation for the oxygen reduction reaction in Fe–N–C catalysts.


2017 ◽  
Vol 56 (48) ◽  
pp. 14172-14181 ◽  
Author(s):  
Jianjun Chen ◽  
Jinxing Mi ◽  
Kezhi Li ◽  
Xiqin Wang ◽  
Elizabeth Dominguez Garcia ◽  
...  

2021 ◽  
Vol 22 (8) ◽  
pp. 3982
Author(s):  
Karolina Kotecka ◽  
Adam Kawalek ◽  
Kamil Kobylecki ◽  
Aneta Agnieszka Bartosik

Pseudomonas aeruginosa is a facultative human pathogen, causing acute and chronic infections that are especially dangerous for immunocompromised patients. The eradication of P. aeruginosa is difficult due to its intrinsic antibiotic resistance mechanisms, high adaptability, and genetic plasticity. The bacterium possesses multilevel regulatory systems engaging a huge repertoire of transcriptional regulators (TRs). Among these, the MarR family encompasses a number of proteins, mainly acting as repressors, which are involved in response to various environmental signals. In this work, we aimed to decipher the role of PA3458, a putative MarR-type TR from P. aeruginosa. Transcriptional profiling of P. aeruginosa PAO1161 overexpressing PA3458 showed changes in the mRNA level of 133 genes; among them, 100 were down-regulated, suggesting the repressor function of PA3458. Concomitantly, ChIP-seq analysis identified more than 300 PA3458 binding sites in P. aeruginosa. The PA3458 regulon encompasses genes involved in stress response, including the PA3459–PA3461 operon, which is divergent to PA3458. This operon encodes an asparagine synthase, a GNAT-family acetyltransferase, and a glutamyl aminopeptidase engaged in the production of N-acetylglutaminylglutamine amide (NAGGN), which is a potent bacterial osmoprotectant. We showed that PA3458-mediated control of PA3459–PA3461 expression is required for the adaptation of P. aeruginosa growth in high osmolarity. Overall, our data indicate that PA3458 plays a role in osmoadaptation control in P. aeruginosa.


1997 ◽  
Vol 272 (35) ◽  
pp. 22080-22085 ◽  
Author(s):  
Richard A. Smith ◽  
M. W. Mosesson ◽  
Michael M. Rooney ◽  
Susan T. Lord ◽  
A.U. Daniels ◽  
...  

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