Linked Life Data

15739456

Source:http://linkedlifedata.com/resource/pubmed/id/15739456

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2005-3-2
pubmed:abstractText
The varieties of alpha-amylase denatured with 8.0 mol/L urea and 7.0 mol/L guanidine hydrochloride (GuHCl) solutions and their refolded intermediates were separated and renatured through high performance hydrophobic interaction chromatography (HPHIC). With investigating and comparing the numbers of the refolded intermediates and the bioactivity recovery of renaturation by means of HPHIC, it was found that these are quite different. The results can be attributed to the different denaturation mechanism of alpha-amylase with the two denaturing agents. The numbers of the refolded intermediates of urea-unfolded alpha-amylase were found to be more than that denatured by GuHCl, because GuHCl may make the changes in the surface of alpha-amylase molecules, by contrast, urea may do the changes not only in the surface of the protein, but also in the hydrophobic packet interior of the molecules. The HPHIC packings with weak hydrophobicity was found to have good separation efficiency and to have almost continuous and many peaks denoting these intermediates, while that with strong hydrophobicity was found to have higher bioactivity recovery. The numbers of the intermediates of urea-unfolded alpha-amylase were much more than that of bovine pancreatic trypsin inhibitor (BPTI) separated by Weissman et al. The effect of temperature on the separations and the renaturations were investigated too. The result showed that the higher the column temperature, the more the refolded intermediates of unfolded alpha-amylase separated and the lower bioactivity recovery were obtained from HPHIC.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1000-8713
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
284-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
[Investigation of alpha-amylase denatured by urea and guanidine hydrochloride. I. Studies on denaturation mechanism and renaturation efficiency by high-performance hydrophobic interaction chromatography].
pubmed:affiliation
Institute of Modern Separation Science, Northwest University, Xi'an, 710069.
pubmed:publicationType
Journal Article, English Abstract, Research Support, Non-U.S. Gov't, Evaluation Studies