Linked Life Data

1687981

Source:http://linkedlifedata.com/resource/pubmed/id/1687981

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1992-8-26
pubmed:abstractText
Tyrosine hydroxylase was purified in high yield from rat PC12 cells. This three-day procedure consisted of differential ammonium sulfate precipitation, anion-exchange chromatography, and heparin-Sepharose affinity chromatography. It yielded an average of 15 mg of purified protein from 100 flasks of PC12 cells, with greater than 40% recovery of tyrosine hydroxylase. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis yielded a single protein band with a molecular weight of approximately 60,000. The protein had a specific activity of 670 nmol/min/mg and had a Km for its reducing cofactor tetrahydrobiopterin of 1.8 mM. The purified protein can be phosphorylated and activated by cyclic AMP-dependent protein kinase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1046-5928
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10-4
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Tyrosine hydroxylase purification from rat PC12 cells.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Louisiana State University Medical Center, New Orleans 70119.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.