Linked Life Data

10641135

Source:http://linkedlifedata.com/resource/pubmed/id/10641135

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2000-2-14
pubmed:abstractText
Crude shock proteins extracted by two stage osmotic shock were further purified by affinity chromatography to obtain ligand (phenylalanine) specific binding protein (phebip) a component of phenylalanine (phe) transport system from wild type and a phe transport mutant fpaD11 of Aspergillus nidulans. A new eluent 0.1 M Tris-HCl containing 1.5 N NaCl and 0.5 N Na2CO3, pH 8 was used during the investigation. The elution profile of mutant phebip exhibited one simple and two compound peaks instead of three simple ones as exhibited by the wild type phebip. SDS-PAGE profile of mutant phebip showed faster electrophoretic mobility than that of wild type one. It is therefore evident that the mutant phebip has reduced molecular mass (M(r)) due to deletion of a segment that somehow has bearing on the binding capacity of the active site of phebip. The resultant erosion in the binding capacity of the mutant phebip is in turn responsible for its incapability to stimulate transport of ligand across the plasma membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0019-5189
pubmed:author
pubmed:issnType
Print
pubmed:volume
37
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
152-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Phenylalanine transport in Aspergillus nidulans: demonstration of role of phenylalanine binding proteins.
pubmed:affiliation
Microbial and Molecular Genetics Laboratory, Patna University, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't