About: The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants

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About: The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants Goto Sponge NotDistinct Permalink

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scientific article published on 01 October 1989

Attributes	Values
rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в жовтні 1989 (uk) im Oktober 1989 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'ochobre de 1989 (ast) scientific article published on 01 October 1989 (en)
publication date	wds:Q57114596-FDF54234-A18C-4E31-884C-EF3626426EF0
publication date	1989-10-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57114596-90FA5275-4054-459F-B380-536FBB130E12
language of work or name	English
cites work	wds:Q57114596-2CC2E6F3-3547-42F1-BF5C-6ED1B9830CF1 wds:Q57114596-416EBFFD-EFF3-4E95-9CA9-3D7D7E2611B0 wds:Q57114596-596B2876-129E-4C2E-99FA-B5465F2B4DBA wds:Q57114596-5E592ECA-FF9B-4781-B3D3-AE37BF63C805 wds:Q57114596-684AF935-7D18-4C40-B4F4-B7DBFCD05D6F wds:Q57114596-6CB0822B-D2BB-46E4-955B-1DD2253C5D92 wds:Q57114596-7653DE02-2C32-4864-BCD2-8FC18AD385D8 wds:Q57114596-A6ABF255-B609-4B25-A2FD-04F9695761F7 wds:Q57114596-B55CB00E-7819-4394-ACC3-8AB4E7F6D9B5 wds:Q57114596-B8191C87-2775-435F-A71D-F05EBE483871 wds:Q57114596-DDC707B1-9164-4F75-9E8B-A2629E304150 wds:Q57114596-E321EBD5-49EE-455D-B26C-4106E2A4152B wds:Q57114596-FFFDEB6F-7424-466B-9A10-79C95743794C
cites work	The Effects of Polyhydric and Monohydric Alcohols on the Heat Induced Reversible Denaturation of Chymotrypsinogen A The denatured states of lysozyme. Cold denaturation of staphylococcal nuclease The effect of polyhydric and monohydric alcohols on the heat-induced reversible denaturation of lysozyme and ribonuclease The thermodynamics of protein stability. Cold destabilization as a general phenomenon. Low-temperature unfolding of a mutant of phage T4 lysozyme. 1. Equilibrium studies. Nucleation rates of ice in undercooled water and aqueous solutions of polyethylene glycol Freeze denaturation of enzymes and its prevention with additives A comparison of the denatured states of alpha-lactalbumin and lysozyme New trends in cryoenzymology: I.-Supercooled aqueous solutions Supercooled water as medium for enzyme reactions at subzero temperatures Protein folding in cryosolvents and at subzero temperatures Structure and function of carboxypeptidase A alpha in supercooled water
author name string	wds:Q57114596-835FC1E7-B35D-404E-A443-9EBDF8484019 wds:Q57114596-9AB38F88-FF2E-495E-AD13-003F26E8D70F
author name string	Franks F Hatley RH
rdfs:label	The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants (en) The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants (nl)
skos:prefLabel	The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants (en) The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants (nl)
name	The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants (en) The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants (nl)
title	wds:Q57114596-AB9EEF40-985E-4066-AE23-C7A287E0DB4B
title	The cold-induced denaturation of lactate dehydrogenase at sub-zero temperatures in the absence of perturbants (en)
page(s)	wds:Q57114596-CFF6CAAF-82C9-4228-A71E-77B567C71A09
page(s)	171-173
instance of	wds:Q57114596-C2180377-D2E1-4F39-ABB2-60C670D6109C
instance of	scholarly article
main subject	wds:Q57114596-9C3F636E-BB5F-4CD2-8F0F-E03BB5BBBD02
main subject	denaturation
PubMed ID	wds:Q57114596-40C5D239-2826-4139-BD7B-0D382ADC32DE
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2806559
PubMed ID	2806559
published in	wds:Q57114596-0C01EA5D-FB05-400E-9935-FD5F33577608
published in	FEBS Letters
issue	wds:Q57114596-EAB4AC0D-9D3C-416D-8367-A03D61076772
volume	wds:Q57114596-F55C084D-6278-46A7-8B27-BA7C6CFA44C8
issue	1
volume	257
DOI	wds:Q57114596-CBEF7E02-7740-444A-BB61-57A23E834793
DOI	http://dx.doi.org/10.1016/0014-5793(89)81813-7
DOI	10.1016/0014-5793(89)81813-7
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57114596
is cites work of	Cold denaturation and 2H2O stabilization of a staphylococcal nuclease mutant Protein stability: the value of 'old literature'. Direct access to the cooperative substructure of proteins and the protein ensemble via cold denaturation Stabilization of lactate dehydrogenase following freeze thawing and vacuum-drying in the presence of trehalose and borate. Evaluation of a new immunoassay for chromogranin A measurement on the Kryptor system. Considerations on Protein Stability During Freezing and Its Impact on the Freeze-Drying Cycle: A Design Space Approach Adsorbing/dissolving Lyoprotectant Matrix Technology for Non-cryogenic Storage of Archival Human Sera Inhomogeneous Distribution of Components in Solid Protein Pharmaceuticals: Origins, Consequences, Analysis, and Resolutions
is cites work of	wds:Q30330377-4395EDCC-6962-4EDB-B5AD-59325964E35F wds:Q53802963-E14BB6A1-ACC9-4506-827B-8699D92B9257 wds:Q90923443-6E56E5B9-0B6E-409E-A1C5-076D103488B8 wds:Q47678830-94C4898F-9231-4DCC-B2FF-B62F073E9889 wds:Q30909229-8A3B62B1-4B78-48FF-AB8D-EC14CB803ABC wds:Q90672126-15631195-BE57-4A6A-9669-BF4483F8AA21 wds:Q31033948-3442799C-FEFB-4597-843B-693BEC5A94E9 wds:Q36789976-13777F05-DC9E-4BDF-A8BA-C8C563AF8D03

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