Linked Life Data

2199832

Source:http://linkedlifedata.com/resource/pubmed/id/2199832

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1990-9-10
pubmed:abstractText
Recent data on the structure and chemical modification of the two main storage proteins of rapeseed, the high-molecular mass 12 S globulin and the low-molecular mass 2 S protein (napin) are summarized and compared with those of related seed proteins. The 12 S globulin is built up of six subunits forming a quaternary structure which can be approximated by the model of a trigonal antiprism. The subunits, composed of a larger and a smaller polypeptide chain each, have a two-domain structure which is typical for all related plant proteins. These are characterized by a sedimentation coefficient of 11-13 S, a molecular mass of 300,000-360,000 g/mol and a high percentage of beta-sheet conformation. Increasing succinylation results in a step-by-step dissociation up to the subunits and to an unfolding of the latter at a critical level of modification amounting to 60-70%. These structural changes affect the functional properties remarkably. The napin fraction comprises a group of closely related and highly basic proteins with molecular masses of 12,000-14,000 g/mol, a high content of sulphur-containing amino acids and rich in helical conformation. They are built up of a larger and a smaller disulphide bridged polypeptide chain. Acylation does not abolish the secondary or tertiary structure which are stabilized by inter- and intrachain disulphide bonds. Acylation results, however, in a stabilization of the protein against heat-induced aggregation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0027-769X
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
225-40
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins.
pubmed:affiliation
Central Institute of Nutrition in Potsdam-Rehbrücke, Academy of Sciences of the GDR.
pubmed:publicationType
Journal Article, Review