scholarly journals Discontinuous Force Compression Curve of Single Bovine Carbonic Anhydrase Molecule Originated from Atomistic Slip

2006 ◽  
Vol 4 ◽  
pp. 552-558 ◽  
Author(s):  
Katsunori Tagami ◽  
Masaru Tsukada ◽  
Rehana Afrin ◽  
Hiroshi Sekiguchi ◽  
Atsushi Ikai
Keyword(s):  
Carbonic Anhydrase ◽  
Compression Curve ◽  
Bovine Carbonic Anhydrase

Characterization of cobalt(II) bovine carbonic anhydrase and of its derivatives

1978 ◽  
Vol 100 (15) ◽  
pp. 4873-4877 ◽  
Author(s):  
I. Bertini ◽  
G. Canti ◽  
C. Luchinat ◽  
A. Scozzafava
Keyword(s):  
Carbonic Anhydrase ◽  
Bovine Carbonic Anhydrase

ChemInform Abstract: BISDIPYRIDYL COPPER(II) IODIDE AS A PENTACOORDINATE MODEL OF THE COPPER(II) BOVINE CARBONIC ANHYDRASE IODIDE COMPLEX

1978 ◽  
Vol 9 (40) ◽  
Author(s):  
L. MORPURGO ◽  
R. FALCIONI ◽  
G. ROTILIO ◽  
A. DESIDERI ◽  
B. MONDOVI
Keyword(s):  
Carbonic Anhydrase ◽  
Bovine Carbonic Anhydrase ◽  
Iodide Complex

Zinc effect on physical properties of bovine carbonic anhydrase

1968 ◽  
Vol 168 (2) ◽  
pp. 359-361 ◽  
Author(s):  
J.M. Brewer ◽  
T.E. Spencer ◽  
R.B. Ashworth
Keyword(s):  
Carbonic Anhydrase ◽  
Physical Properties ◽  
Bovine Carbonic Anhydrase

scholarly journals Protein Folding by Domain V of Escherichia coli 23S rRNA: Specificity of RNA-Protein Interactions

2008 ◽  
Vol 190 (9) ◽  
pp. 3344-3352 ◽  
Author(s):  
Dibyendu Samanta ◽  
Debashis Mukhopadhyay ◽  
Saheli Chowdhury ◽  
Jaydip Ghosh ◽  
Saumen Pal ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Folding ◽  
Carbonic Anhydrase ◽  
Protein Interactions ◽  
23S Rrna ◽  
Unfolded Proteins ◽  
Bovine Carbonic Anhydrase ◽  
Egg White Lysozyme ◽  
General Protein ◽  
Domain V

ABSTRACT The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to unfolded proteins and, as shown previously, bring the trapped proteins to a folding-competent state before releasing them. These nucleotides are the same for the proteins studied so far: bovine carbonic anhydrase, lactate dehydrogenase, malate dehydrogenase, and chicken egg white lysozyme. The amino acids that interact with these nucleotides are also found to be specific in the two cases tested: bovine carbonic anhydrase and lysozyme. They are either neutral or positively charged and are present in random coils on the surface of the crystal structure of both the proteins. In fact, two of these amino acid-nucleotide pairs are identical in the two cases. How these features might help the process of protein folding is discussed.

Two slow stages in refolding of bovine carbonic anhydrase B are due to proline isomerization

1990 ◽  
Vol 213 (3) ◽  
pp. 561-568 ◽  
Author(s):  
G.V. Semisotnov ◽  
V.N. Uversky ◽  
I.V. Sokolovsky ◽  
A.M. Gutin ◽  
O.I. Razgulyaev ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Bovine Carbonic Anhydrase ◽  
Proline Isomerization ◽  
Carbonic Anhydrase B

Formation of amyloid fibrils by bovine carbonic anhydrase

2008 ◽  
Vol 1784 (6) ◽  
pp. 930-935 ◽  
Author(s):  
Anshul Rana ◽  
Teemish Praveen Gupta ◽  
Saurabh Bansal ◽  
Bishwajit Kundu
Keyword(s):  
Carbonic Anhydrase ◽  
Amyloid Fibrils ◽  
Bovine Carbonic Anhydrase

Extracellular carbonic anhydrase of skeletal muscle associated with the sarcolemma

1985 ◽  
Vol 59 (2) ◽  
pp. 548-558 ◽  
Author(s):  
C. Geers ◽  
G. Gros ◽  
A. Gartner
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Plasma Membranes ◽  
Oxidative Capacity ◽  
Carbonic Anhydrase Ii ◽  
Histochemical Technique ◽  
Bovine Carbonic Anhydrase ◽  
Molecular Weights ◽  
Strong Staining ◽  
Bovine Carbonic Anhydrase Ii

We report here 1) the synthesis and properties of a new macromolecular carbonic anhydrase inhibitor, Prontosil-dextran, 2) its application to determine the localization of a previously described extracellular carbonic anhydrase in skeletal muscle, and 3) the application of a recently published histochemical technique using dansylsulfonamide to the same problem. Stable macromolecular inhibitors of molecular weights of 5,000, 100,000 and 1,000,000 were produced by covalently coupling the sulfonamide Prontosil to dextrans. Their inhibition constants towards bovine carbonic anhydrase II are 1–2 X 10(-7) M. The Prontosil-dextrans, PD 5,000, PD 100,000, and PD 1,000,000, were used in studies of the washout of H14CO3-) from the perfused rabbit hindlimb. This washout is slow due to the presence of an extracellular carbonic anhydrase and can be markedly accelerated by PD 5,000 but not by PD 100,000 and PD 1,000,000. Since PD 5,000 is accessible to the entire extracellular space and PD 100,000 and PD 1,000,000 are confined to the intravascular space, we conclude that the extracellular carbonic anhydrase of skeletal muscle is located in the interstitium. The histochemical studies show a strong staining of the sarcolemma of the muscle fibers with high oxidative capacity. It appears likely, therefore, that the extracellular carbonic anhydrase of skeletal muscle is associated with muscle plasma membranes with its active site directed toward the interstitial space.

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