|   | 
Details
   web
Records
Author Alexander, F.; Davies, M.E.
Title Production and fermentation of lactate by bacteria in the alimentary canal of the horse and pig Type Journal Article
Year 1963 Publication Journal of comparative pathology Abbreviated Journal J Comp Pathol
Volume 73 Issue Pages 1-8
Keywords *Fatty Acids; Intestines/*microbiology; *Lactates; *Lactobacillus; *Stomach; *Urea; *Veillonella; *Fatty Acids; *Intestinal Microorganisms; *Lactates; *Lactobacillus; *Stomach; *Urea; *Veillonella
Abstract
Address
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0021-9975 ISBN Medium
Area Expedition Conference
Notes PMID:14011947 Approved no
Call Number refbase @ user @ Serial 120
Permanent link to this record
 

 
Author Chiba, K.; Ikai, A.; Kawamura-Konishi, Y.; Kihara, H.
Title Kinetic study on myoglobin refolding monitored by five optical probe stopped-flow methods Type Journal Article
Year 1994 Publication Proteins Abbreviated Journal Proteins
Volume 19 Issue 2 Pages 110-119
Keywords Animals; Chromatography, Gel; Circular Dichroism; Horses; Kinetics; Metmyoglobin/analogs & derivatives/chemistry; Myoglobin/*chemistry; *Protein Folding; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Urea
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.
Address Laboratory of Biodynamics, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Kanagawa, Japan
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0887-3585 ISBN Medium
Area Expedition Conference
Notes PMID:8090705 Approved no
Call Number Equine Behaviour @ team @ Serial 3799
Permanent link to this record
 

 
Author Gabris, G.T.; Ihrke, D.M.
Title No End to Hierarchy: Does Rank Make a Difference in Perceptions of Leadership Credibility? Type Journal Article
Year 2007 Publication Administration Society Abbreviated Journal Admin. Soc.
Volume 39 Issue 1 Pages 107-123
Keywords hierarchy; leadership; credibility; culture; bureaucracy
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.
Address
Corporate Author Thesis
Publisher Place of Publication Editor
Language Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN ISBN Medium
Area Expedition Conference
Notes Approved no
Call Number Equine Behaviour @ team @ Serial 4804
Permanent link to this record
 

 
Author Houpt, T.R.; Houpt, K.A.
Title Nitrogen conservation by ponies fed a low -protein ration Type Journal Article
Year 1971 Publication American journal of veterinary research Abbreviated Journal Am J Vet Res
Volume 32 Issue 4 Pages 579-588
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
Abstract
Address
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0002-9645 ISBN Medium
Area Expedition Conference
Notes PMID:5110116 Approved no
Call Number refbase @ user @ Serial 62
Permanent link to this record
 

 
Author Tsong, T.Y.
Title Conformational relaxations of urea- and guanidine hydrochloride-unfolded ferricytochrome c Type Journal Article
Year 1977 Publication The Journal of Biological Chemistry Abbreviated Journal J Biol Chem
Volume 252 Issue 24 Pages 8778-8780
Keywords *Cytochrome c Group; Guanidines/*pharmacology; Protein Conformation/drug effects; Spectrometry, Fluorescence; Urea/*pharmacology
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.
Address
Corporate Author Thesis
Publisher Place of Publication Editor
Language English Summary Language Original Title
Series Editor Series Title Abbreviated Series Title
Series Volume Series Issue Edition
ISSN 0021-9258 ISBN Medium
Area Expedition Conference
Notes PMID:200618 Approved no
Call Number refbase @ user @ Serial 3882
Permanent link to this record