Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-11-24
pubmed:abstractText
We have developed a one chromatographic step isolation protocol for the neuron specific protein synapsin I. This procedure results in a yield of 80 micrograms/g brain, which is ten fold better than the highest yield yet reported for this protein. The authenticity of the synapsin I isolated by this procedure is demonstrated by comigration with authentic synapsin I on SDS-polyacrylamide gels, crossreactivity with antibody specific against synapsin I, and nearly identical two dimensional chrymotryptic iodopeptide maps of authentic synapsin I and the protein purified by this protocol. Synapsin I isolated by this procedure retains its functional properties, demonstrated by the ability of synapsin I to stimulate the formation of a brain spectrin(240/235)/synapsin I/F-actin ternary complex as determined by a low shear falling ball viscometry assay. This novel protocol therefore has the advantage of being a rapid, high yield procedure that retains the functional properties of synapsin I.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0361-9230
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
237-41
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
A rapid purification of synapsin I: a neuron specific spectrin binding protein.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't