Spectroscopic Evidence for a Conformational Transition in Horseradish Peroxidase at Very Low pH†

Biochemistry ◽  
1997 ◽  
Vol 36 (3) ◽  
pp. 640-649 ◽  
Author(s):  
Giulietta Smulevich ◽  
Mauro Paoli ◽  
Giampiero De Sanctis ◽  
Anna Rita Mantini ◽  
Franca Ascoli ◽  
...  

1990 ◽  
Vol 38 (12) ◽  
pp. 1927-1931 ◽  
Author(s):  
E Augenbraun ◽  
D Sulzer ◽  
S Rayport ◽  
W Setlik ◽  
E Holtzman

Immunocytochemical localization of DAMP, a reagent used to detect low pH intracellular compartments, was studied in cultured neurons from rat hippocampus and in frog retinas. We find that DAMP is more sharply localized and that the immunocytochemical reaction is stronger when horseradish peroxidase or other proteins are included in the medium used to administer DAMP to the cells. A likely explanation is that the proteins enter acidified endocytic compartments and there provide sites to which DAMP molecules can be attached during fixation.



2014 ◽  
Vol 18 (03) ◽  
pp. 231-239 ◽  
Author(s):  
Janet L. Shaw ◽  
Jonathan L. McMurry ◽  
Pooya Salehi ◽  
Alexander Stovall

The acid-base and aggregation behavior of water soluble meso-tetrakis(p-sulfonato-phenyl)N-confused porphyrin was explored using UV-visible spectroscopy. Stepwise protonation events were observed in acidic media with pK4 = 5.8 and pK3 = 7.7, and spectroscopic evidence suggests the formation of polymeric aggregates at low pH. meso-tetrakis(p-sulfonatophenyl)N-confused porphyrin was found to obey Beer's Law in dimethylformamide and methanol over the concentration range of 10-4 to 10-6 M and at low concentration in water. Deviations in water at higher concentration were analyzed to determine KD values for aggregate formation in the presence and absence of salt and buffer.



2001 ◽  
Vol 6 (4) ◽  
pp. 348-358 ◽  
Author(s):  
P. John Wright ◽  
Ann M. English


2002 ◽  
Vol 66 (3) ◽  
pp. 651-654 ◽  
Author(s):  
Tomonori KAWANO ◽  
Shoshi MUTO ◽  
Masaru ADACHI ◽  
Hiroshi HOSOYA ◽  
Frédéric LAPEYRIE


Biochemistry ◽  
1969 ◽  
Vol 8 (10) ◽  
pp. 4159-4162 ◽  
Author(s):  
Thomas H. Moss ◽  
Anders Ehrenberg ◽  
Alan J. Bearden


2000 ◽  
Vol 79 (1-4) ◽  
pp. 25-30 ◽  
Author(s):  
Anna Maria Priori ◽  
Chiara Indiani ◽  
Giampiero De Sanctis ◽  
Stefano Marini ◽  
Roberto Santucci ◽  
...  




1995 ◽  
Vol 249 (4) ◽  
pp. 800-803 ◽  
Author(s):  
Massimo Coletta ◽  
Paolo Ascenzi ◽  
Massimo Castagnola ◽  
Bruno Giardina


2014 ◽  
Vol 70 (11) ◽  
pp. 1498-1503 ◽  
Author(s):  
George Kontopidis ◽  
Anna Nordle Gilliver ◽  
Lindsay Sawyer

The crystal structure of the triclinic form of the milk protein β-lactoglobulin from sheep (Ovis aries) at 1.1 Å resolution is described together with a comparison of the triclinic structures of the low-pH bovine and high-pH ovine proteins. All three structures are remarkably similar, despite the well known pH-dependent conformational transition described for the bovine and porcine proteins that occurs in solution. The high resolution of the present structure determination has allowed a more accurate description of the protein than has hitherto been possible, but it is still not clear whether flexibility changes in the external loops can compensate for the presence of a significant void in the unliganded interior of the structure.



2011 ◽  
Vol 65 (6) ◽  
Author(s):  
Jiří Horský ◽  
Jiří Podešva ◽  
Zuzana Walterová

AbstractA pH-induced conformational transition of atactic poly(2-methylprop-2-enoic acid) (poly(methacrylic acid), PMMA) from the contracted to expanded conformation was investigated by viscometry, potentiometric titration, and anthracene solubilisation in the presence of low-molecular-mass non-ionogenic co-solutes-glucose, α-cyclodextrin (αCD), and γ-cyclodextrin (γCD), respectively. No effect of glucose and αCD on the conformational transition was observed with either of the methods used. On the other hand, the characteristic features of the conformational transition were absent in the presence of γCD. The different effects of the co-solutes indicate that the interaction between PMAA and γCD corresponds to the partial inclusion of the PMAA chain into the γCD cavity. The viscometry and anthracene solubilisation imply that γCD promotes the expanded conformation of PMAA at low pH. The potentiometric titration does not support this conclusion. Even though there is no break on the Henderson-Hasselbalch plot, a characteristic of the conformational transition, the potentiometric behaviour corresponds to that of the contracted PMMA conformation. Thus the results suggest the hierarchical picture of the PMAA conformation at low pH in which the local arrangement of the PMAA chain is a prerequisite for clustering on a larger scale.



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