Linked Life Data

7119782

Source:http://linkedlifedata.com/resource/pubmed/id/7119782

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1982-12-2
pubmed:abstractText
Dopamine beta-hydroxylase (DBH) was purified from bovine brain by a series of steps including extraction with 0.5% Triton X-100, ammonium sulfate fractionation, and serial chromatographies with Concanavalin A (Con A)-Sepharose, Biogel A-1.5 m, DEAE-Sephadex, and phenyl-Sepharose. The overall purification was approximately 4200-fold and the final specific activity was 147 nmol/min/mg protein. Bovine brain DBH was apparently a glycoprotein and interacted with immobilized Con A. Furthermore, the enzyme bound to phenyl-substituted agarose by hydrophobic interaction. An approximate molecular weight was estimated to be 400,000 by gel filtration; the protein eluted earlier than bovine adrenal DBH with a molecular weight estimated to be 290,000. The Km values toward tyramine and ascorbate were 1.53 and 1.42 mM, respectively, the optimal pH was 5.0 in the presence of 20 mM tyramine as substrate. Immunological titration studies indicated that bovine brain and adrenal DBH had common antigenic sites. Our data showed a close similarity between the bovine brain and adrenal enzymes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-3042
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1066-71
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Purification and properties of bovine brain dopamine beta-hydroxylase.
pubmed:publicationType
Journal Article