Linked Life Data

3156853

Source:http://linkedlifedata.com/resource/pubmed/id/3156853

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1985-5-3
pubmed:abstractText
The complex nature of the brain 6-phosphofructo-1-kinase isozymes was examined by elution with a discontinuous gradient from QAE (quaternary aminoethyl)-Sephadex. In the first wash (150 mM NaCl), where the rat muscle 6-phosphofructo-1-kinase isozyme (M4) eluted, about 40% of the total brain 6-phosphofructo-1-kinase activity washed through without exhibiting a sharp peak. In the second elution (300 mM NaCl), the remaining activity eluted in a sharp peak that preceded where the major rat liver 6-phosphofructo-1-kinase isozyme (L4) eluted. Enzyme activity in brain extracts or purified brain isozymes was titrated above 90% with M4 anti-IgG and 20% with L4 anti-IgG. A purification procedure was developed which resulted in a recovery of 70 to 80% of the original enzyme activity in brain 100,000 X g supernatant fluids. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis on slab gels and detection by silver staining indicated that three components were present with apparent molecular weights of 87,500, 85,000, and 80,000. The 85,000- and 80,000-dalton components corresponded to the subunits of M4 and L4, respectively. The third component (C type) was thought to be an actual subunit since it exhibited the highest molecular weight and was present in an exhaustively washed immunoprecipitate of the purified brain isozymes. From 10 different purifications of the brain enzyme, the subunit distributions of the liver, muscle, and C-type subunit were 1.4 +/- 0.2, 4.9 +/- 0.5, and 3.9 +/- 0.3, respectively. A comparison of the kinetic properties of purified liver, muscle, and brain isozymes clearly demonstrated that all three preparations had quantitatively different regulatory properties. All three subunits were present in different regions of the brain, and region-specific changes in total activity and the relative amounts of each subunit were observed. This study suggests that brain 6-phosphofructo-1-kinase is a complex mixture of homotetramers and hybrids which are composed of different amounts of the three subunits.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
260
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4180-5
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Nature of the rat brain 6-phosphofructo-1-kinase isozymes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't