| Records |
Author  |
Aviad, A.D.; Houpt, J.B. |
| Title |
The molecular weight of therapeutic hyaluronan (sodium hyaluronate): how significant is it? |
Type |
Journal Article |
| Year |
1994 |
Publication |
The Journal of rheumatology |
Abbreviated Journal |
J Rheumatol |
| Volume |
21 |
Issue |
2 |
Pages |
297-301 |
| Keywords |
Animals; Horse Diseases/drug therapy; Horses; Humans; Hyaluronic Acid/*chemistry/*therapeutic use; Joint Diseases/*drug therapy/veterinary; Molecular Weight; Osteoarthritis/drug therapy/veterinary; Synovial Fluid/drug effects/physiology; Viscosity |
| Abstract |
Various molecular weight hyaluronic acid (HA) preparations have been injected into joints for the treatment of human and equine osteoarthritis. A therapeutic advantage has been claimed for commercial products with a molecular weight in the range found in normal synovial fluid (SF), compared to lower molecular weight products. But a correlation between molecular weight and efficacy is not borne out by an analysis of the available literature on clinical results. SF viscosity, HA concentration, HA molecular weight and rate of synthesis in joint disease. It is proposed that the beneficial effect of injected HA in joint disease may be due to pharmacological rather than to physical properties. |
| Address |
Rheumatic Disease Unit, Mount Sinai Hospital, University of Toronto, ON, Canada |
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English |
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| ISSN |
0315-162X |
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| Notes |
PMID:8182640 |
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no |
| Call Number |
refbase @ user @ |
Serial |
35 |
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| Author |
Anderson, W.D.; Summers, C.H. |
| Title |
Neuroendocrine Mechanisms, Stress Coping Strategies, and Social Dominance: Comparative Lessons about Leadership Potential |
Type |
Journal Article |
| Year |
2007 |
Publication |
The ANNALS of the American Academy of Political and Social Science |
Abbreviated Journal |
Ann Am Acad Polit Soc Sci |
| Volume |
614 |
Issue |
1 |
Pages |
102-130 |
| Keywords |
social dominance – authoritarian – Five Factor Model – neurochemistry – neurotransmitters – leadership |
| Abstract |
The authors examine dominance and subordination in the social psychology, political science, and biology literatures. Using Summers and Winberg (2006) as a guide, the authors suggest that extreme dominance or subordination phenotypes--including social dominance orientation and right-wing authoritarianism--are determined by an organism's genetic predispositions, motivations, stress responses, and long-term hormone release and uptake states. The authors offer hypotheses about the likely neurochemical profiles for each of these extreme dominance and subordination phenotypes and suggest two designs that begin to test these hypotheses. |
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Equine Behaviour @ team @ |
Serial |
4699 |
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| Author |
Abbruzzetti, S.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
| Title |
Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique |
Type |
Journal Article |
| Year |
2001 |
Publication |
Journal of the American Chemical Society |
Abbreviated Journal |
J Am Chem Soc |
| Volume |
123 |
Issue |
27 |
Pages |
6649-6653 |
| Keywords |
Animals; *Bacterial Proteins; Cytochrome c Group/*chemistry; Guanidine/*chemistry; Heme/*chemistry; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; *Lasers; Ligands; Protein Folding |
| Abstract |
We have developed an instrumental setup that uses transient absorption to monitor protein folding/unfolding processes following a laser-induced, ultrafast release of protons from o-nitrobenzaldehyde. The resulting increase in [H(+)], which can be more than 100 microM, is complete within a few nanoseconds. The increase in [H(+)] lowers the pH of the solution from neutrality to approximately 4 at the highest laser pulse energy used. Protein structural rearrangements can be followed by transient absorption, with kinetic monitoring over a broad time range (approximately 10 ns to 500 ms). Using this pH-jump/transient absorption technique, we have examined the dissociation kinetics of non-native axial heme ligands (either histidine His26 or His33) in GuHCl-unfolded Fe(III) cytochrome c (cyt c). Deligation of the non-native ligands following the acidic pH-jump occurs as a biexponential process with different pre-exponential factors. The pre-exponential factors markedly depend on the extent of the pH-jump, as expected from differences in the pK(a) values of His26 and His33. The two lifetimes were found to depend on temperature but were not functions of either the magnitude of the pH-jump or the pre-pulse pH of the solution. The activation energies of the deligation processes support the suggestion that GuHCl-unfolded cyt c structures with non-native histidine axial ligands represent kinetic traps in unfolding. |
| Address |
Dipartimento di Fisica, Universita di Parma, Istituto Nazionale per la Fisica della Materia, 43100 Parma, Italy |
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English |
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0002-7863 |
ISBN |
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| Notes |
PMID:11439052 |
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no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3788 |
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| Author |
Abbruzzetti, S.; Viappiani, C.; Sinibaldi, F.; Santucci, R. |
| Title |
Kinetics of histidine dissociation from the heme Fe(III) in N-fragment (residues 1-56) of cytochrome c |
Type |
Journal Article |
| Year |
2004 |
Publication |
The Protein Journal |
Abbreviated Journal |
Protein J |
| Volume |
23 |
Issue |
8 |
Pages |
519-527 |
| Keywords |
Animals; Cytochromes c/*chemistry; Enzyme Activation; Histidine/*chemistry; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Peptide Mapping; Photolysis; Spectrophotometry |
| Abstract |
We have here investigated the dissociation kinetics of the His side chains axially ligated to the heme-iron in the ferric (1-56 residues) N-fragment of horse cyt c. The ligand deligation induced by acidic pH-jump occurs as a biexponential process with different pre-exponential factors, consistent with a structural heterogeneity in solution and the presence of two differently coordinated species. In analogy with GuHCl-denatured cyt c, our data indicate the presence in solution of two ferric forms of the N-fragment characterized by bis-His coordination, as summarized in the following scheme: His18-Fe(III)-His26 <==> His18-Fe(III)-His33. We have found that the pre-exponential factors depend on the extent of the pH-jump. This may be correlated with the different pKa values shown by His26 and His33; due to steric factors, His26 binds to the heme-Fe(III) less strongly than His33, as recently shown by studies on denatured cyt c. Interestingly, the two lifetimes are affected by temperature but not by the extent of the pH-jump. The lower pKa for the deligation reaction required the use of an improved laser pH-jump setup, capable of inducing changes in H+ concentration as large as 1 mM after the end of the laser pulse. For the ferric N-fragment, close activation entropy values have been determined for the two histidines coordinated to the iron; this result significantly differs from that for GuHCl-denatured cyt c, where largely different values of activation entropy were calculated. This underlines the role played by the missing segment (residues 57-104) peptide chain in discriminating deligation of the “nonnative” His from the sixth coordination position of the metal. |
| Address |
Dipartimento di Fisica, Universita degli Studi di Parma, Parco Area delle Scienze 7/A 43100 Parma, Italy |
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English |
Summary Language |
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Edition |
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| ISSN |
1572-3887 |
ISBN |
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| Notes |
PMID:15648974 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3770 |
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| Author |
Abbruzzetti, S.; Crema, E.; Masino, L.; Vecli, A.; Viappiani, C.; Small, J.R.; Libertini, L.J.; Small, E.W. |
| Title |
Fast events in protein folding: structural volume changes accompanying the early events in the N-->I transition of apomyoglobin induced by ultrafast pH jump |
Type |
Journal Article |
| Year |
2000 |
Publication |
Biophysical Journal |
Abbreviated Journal |
Biophys J |
| Volume |
78 |
Issue |
1 |
Pages |
405-415 |
| Keywords |
Animals; Apoproteins/*chemistry; Horses; *Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Myoglobin/*chemistry; Protein Conformation; *Protein Folding; Protein Structure, Secondary; Spectrometry, Fluorescence |
| Abstract |
Ultrafast, laser-induced pH jump with time-resolved photoacoustic detection has been used to investigate the early protonation steps leading to the formation of the compact acid intermediate (I) of apomyoglobin (ApoMb). When ApoMb is in its native state (N) at pH 7.0, rapid acidification induced by a laser pulse leads to two parallel protonation processes. One reaction can be attributed to the binding of protons to the imidazole rings of His24 and His119. Reaction with imidazole leads to an unusually large contraction of -82 +/- 3 ml/mol, an enthalpy change of 8 +/- 1 kcal/mol, and an apparent bimolecular rate constant of (0.77 +/- 0.03) x 10(10) M(-1) s(-1). Our experiments evidence a rate-limiting step for this process at high ApoMb concentrations, characterized by a value of (0. 60 +/- 0.07) x 10(6) s(-1). The second protonation reaction at pH 7. 0 can be attributed to neutralization of carboxylate groups and is accompanied by an apparent expansion of 3.4 +/- 0.2 ml/mol, occurring with an apparent bimolecular rate constant of (1.25 +/- 0.02) x 10(11) M(-1) s(-1), and a reaction enthalpy of about 2 kcal/mol. The activation energy for the processes associated with the protonation of His24 and His119 is 16.2 +/- 0.9 kcal/mol, whereas that for the neutralization of carboxylates is 9.2 +/- 0.9 kcal/mol. At pH 4.5 ApoMb is in a partially unfolded state (I) and rapid acidification experiments evidence only the process assigned to carboxylate protonation. The unusually large contraction and the high energetic barrier observed at pH 7.0 for the protonation of the His residues suggests that the formation of the compact acid intermediate involves a rate-limiting step after protonation. |
| Address |
Dipartimento di Fisica, Universita di Parma, 43100 Parma, Italia |
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English |
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0006-3495 |
ISBN |
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| Notes |
PMID:10620304 |
Approved |
no |
| Call Number |
Equine Behaviour @ team @ |
Serial |
3792 |
| Permanent link to this record |
