Linked Life Data

8287964

Source:http://linkedlifedata.com/resource/pubmed/id/8287964

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-2-18
pubmed:abstractText
Cholesterol esterase from Candida cylindracea was separated into two fractions, corresponding to a dimeric and a monomeric form. Fingerprint analysis after lysine cleavages shows identical patterns, suggesting lack of primary differences. Crystals obtained from the two proteins differ and suggest the possibility of an equilibrium between the two forms, influenced by the substrate cholesterol linoleate, which appears to stabilize the more active, dimeric form. All crystals have dimers as the asymmetric unit. The primary structure of the enzyme was determined at the peptide level and shows only one difference, Leu-350 instead of Ile, from a DNA-deduced amino acid sequence, and conservation of features typical for cholesterol esterases characterized.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
337
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
123-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Monomeric and dimeric forms of cholesterol esterase from Candida cylindracea. Primary structure, identity in peptide patterns, and additional microheterogeneity.
pubmed:affiliation
Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, Sweden.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't