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Author |
Houpt, T.R.; Houpt, K.A. |
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Title |
Nitrogen conservation by ponies fed a low -protein ration |
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Journal Article |
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Year |
1971 |
Publication |
American journal of veterinary research |
Abbreviated Journal |
Am J Vet Res |
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Volume |
32 |
Issue |
4 |
Pages |
579-588 |
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Keywords |
Administration, Oral; Amino Acids/biosynthesis; Animals; Anti-Infective Agents/pharmacology; Body Weight/drug effects; Dietary Proteins/*pharmacology; Horses/*metabolism; Nitrogen/*metabolism; Urea/administration & dosage/antagonists & inhibitors/metabolism; Water/metabolism |
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0002-9645 |
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PMID:5110116 |
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refbase @ user @ |
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62 |
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Author |
Alexander, F.; Davies, M.E. |
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Title |
Production and fermentation of lactate by bacteria in the alimentary canal of the horse and pig |
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Journal Article |
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Year |
1963 |
Publication |
Journal of comparative pathology |
Abbreviated Journal |
J Comp Pathol |
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Volume |
73 |
Issue |
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Pages |
1-8 |
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Keywords |
*Fatty Acids; Intestines/*microbiology; *Lactates; *Lactobacillus; *Stomach; *Urea; *Veillonella; *Fatty Acids; *Intestinal Microorganisms; *Lactates; *Lactobacillus; *Stomach; *Urea; *Veillonella |
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0021-9975 |
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PMID:14011947 |
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refbase @ user @ |
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120 |
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Author |
Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H. |
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Title |
Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods |
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Journal Article |
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Year |
1994 |
Publication |
Proteins |
Abbreviated Journal |
Proteins |
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Volume |
19 |
Issue |
2 |
Pages |
110-119 |
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Keywords |
Animals; Chromatography, Gel; Circular Dichroism; Horses; Kinetics; Metmyoglobin/analogs & derivatives/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Urea |
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Abstract |
The refolding kinetics of horse cyanometmyoglobin induced by concentration jump of urea was investigated by five optical probe stopped-flow methods: absorption at 422 nm, tryptophyl fluorescence at around 340 nm, circular dichroism (CD) at 222 nm, CD at 260 nm, and CD at 422 nm. In the refolding process, we detected three phases with rate constants of > 1 x 10(2) s-1, (4.5-9.3) s-1, and (2-5) x 10(-3) s-1. In the fastest phase, a substantial amount of secondary structure (approximately 40%) is formed within the dead time of the CD stopped-flow apparatus (10.7 ms). The kinetic intermediate populated in the fastest phase is shown to capture a hemindicyanide, suggesting that a “heme pocket precursor” recognized by hemindicyanide must be constructed within the dead time. In the middle phase, most of secondary and tertiary structures, especially around the captured hemindicyanide, have been constructed. In the slowest phase, we detected a minor structural rearrangement accompanying the ligand-exchange reaction in the fifth coordination of ferric iron. We present a possible model for the refolding process of myoglobin in the presence of the heme group. |
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Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, Japan |
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0887-3585 |
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PMID:8090705 |
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Call Number |
Equine Behaviour @ team @ |
Serial |
3799 |
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Author |
Tsong, T.Y. |
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Title |
Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c |
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Journal Article |
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Year |
1977 |
Publication |
The Journal of Biological Chemistry |
Abbreviated Journal |
J Biol Chem |
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Volume |
252 |
Issue |
24 |
Pages |
8778-8780 |
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Keywords |
*Cytochrome c Group; Guanidines/*pharmacology; Protein Conformation/drug effects; Spectrometry, Fluorescence; Urea/*pharmacology |
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Abstract |
Several recent studies of protein the unfolded proteins. In urea- and guanidine HCl-unfolded ferricytochrome c (horse heart), an acid-induced spin state transformation of the heme group has been detected by the heme absorptions, Trp-59 fluorescence, and the intrinsic viscosity of protein. Kinetics of this second conformational transition, by the temperature jump and stopped flow methods, are complex. One rapid reaction (tau1), pH-independent, occurs in a 50-mus range; the second reaction (tau2), in a 1-ms range, depends linearly upon pH and is faster at the alkaline side; a third reaction (tau3), in a 1-s range, shows a sigmoidal transition at pH 5.1 and is faster at the acidic side. The results are consistent with a kinetic scheme which involves protein conformational changes in the transformation of the heme coordination state. The kinetics, along with previous equilibrium studies, indicate that ligand or charge interactions within a protein molecule are not completely prohibited even in strongly denaturing conditions, such as in high concentrations of urea and guanidine HCl. Thus, local structures of peptide chain associated with these interactions can exist in the unfolded protein. |
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0021-9258 |
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Notes |
PMID:200618 |
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Call Number |
refbase @ user @ |
Serial |
3882 |
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Author |
Gabris, G.T.; Ihrke, D.M. |
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Title |
No End to Hierarchy: Does Rank Make a Difference in Perceptions of Leadership Credibility? |
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Journal Article |
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Year |
2007 |
Publication |
Administration Society |
Abbreviated Journal |
Admin. Soc. |
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Volume |
39 |
Issue |
1 |
Pages |
107-123 |
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Keywords |
hierarchy; leadership; credibility; culture; bureaucracy |
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Abstract |
This article investigates whether authority hierarchy still serves as an important factor influencing employee perceptions toward organizational roles and expected behavior. Results of a study in a federal agency suggest that hierarchy does serve as a significant force influencing employee attitudes toward leadership roles, contrary to the notion that hierarchy will diminish in importance over time. Hierarchy remains a crucial structural force in public organizations and is unlikely to wither away. |
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Equine Behaviour @ team @ |
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4804 |
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