Matches in SemOpenAlex for { <https://semopenalex.org/work/W1566137581> ?p ?o ?g. }
Showing items 1 to 80 of
80
with 100 items per page.
- W1566137581 endingPage "4822" @default.
- W1566137581 startingPage "4815" @default.
- W1566137581 abstract "6-Phosphofructo-1-kinase (phosphofructokinase) (ATP:D-fructose-6-P 1-phosphotransferase, EC 2.7.1.11) can be identified in sheep heart homogenates in two forms, a soluble form and a form bound to the particulate fraction. Homogenates from immediately-dissected hearts have the enzyme in the soluble form, while those collected after a delay have the enzyme bound to the particulate fraction. Aldolase appears to show the same change in its location. Homogenization in a solution with concentrated macromolecular species (20% albumin) results in a greater association of phosphofructokinase and of aldolase to the particulate fraction in homogenates from immediately dissected hearts. Phosphofructokinase activity can be solubilized by two specific means: by high ionic strength, which is dependent upon specific salts; or by low ionic strength, which is dependent upon the presence of phosphofructokinase substrates or modifier ligands. These two means of solubilization are affected differently upon decreasing the pH below 6.9: the solubilization at low ionic strength is prevented, whereas phosphofructokinase is still solubilized by high ionic strength. Under the latter condition, the enzyme is in the inactive dimeric state, which can be activated at an alkaline pH. Myofibrils present in the particulate fraction can account for the binding of phosphofructokinase in heart homogenates. Purified myofibrils, when added to heart supernatant fluids, can bind phosphofructokinase at a slightly acidic pH. Conditions for phosphofructokinase binding to myofibrils, as well as its dissociation, follow what was observed with the binding of phosphofructokinase to the particulate fraction. At an acidic pH, and in the presence of a high concentration of ATP, phosphofructokinase exhibits low activity. However, if phosphofructokinase is assayed under these conditions while bound to myofibrils, the enzyme is activated." @default.
- W1566137581 created "2016-06-24" @default.
- W1566137581 creator A5003802107 @default.
- W1566137581 creator A5077805522 @default.
- W1566137581 creator A5091828771 @default.
- W1566137581 date "1985-04-01" @default.
- W1566137581 modified "2023-09-27" @default.
- W1566137581 title "Heart 6-phosphofructo-1-kinase. Subcellular distribution and binding to myofibrils." @default.
- W1566137581 cites W1062773 @default.
- W1566137581 cites W1499418040 @default.
- W1566137581 cites W1504979389 @default.
- W1566137581 cites W1840325563 @default.
- W1566137581 cites W187649596 @default.
- W1566137581 cites W1912085582 @default.
- W1566137581 cites W1983103640 @default.
- W1566137581 cites W1990831187 @default.
- W1566137581 cites W1996848603 @default.
- W1566137581 cites W2002104842 @default.
- W1566137581 cites W2012319337 @default.
- W1566137581 cites W2017518453 @default.
- W1566137581 cites W2026097883 @default.
- W1566137581 cites W2026513114 @default.
- W1566137581 cites W2027163663 @default.
- W1566137581 cites W2079103139 @default.
- W1566137581 cites W2082210619 @default.
- W1566137581 cites W2084286730 @default.
- W1566137581 cites W2500058840 @default.
- W1566137581 cites W319312714 @default.
- W1566137581 cites W4211064073 @default.
- W1566137581 cites W62208249 @default.
- W1566137581 doi "https://doi.org/10.1016/s0021-9258(18)89144-x" @default.
- W1566137581 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/3157684" @default.
- W1566137581 hasPublicationYear "1985" @default.
- W1566137581 type Work @default.
- W1566137581 sameAs 1566137581 @default.
- W1566137581 citedByCount "23" @default.
- W1566137581 crossrefType "journal-article" @default.
- W1566137581 hasAuthorship W1566137581A5003802107 @default.
- W1566137581 hasAuthorship W1566137581A5077805522 @default.
- W1566137581 hasAuthorship W1566137581A5091828771 @default.
- W1566137581 hasBestOaLocation W15661375811 @default.
- W1566137581 hasConcept C110121322 @default.
- W1566137581 hasConcept C12554922 @default.
- W1566137581 hasConcept C134306372 @default.
- W1566137581 hasConcept C185592680 @default.
- W1566137581 hasConcept C33923547 @default.
- W1566137581 hasConcept C55493867 @default.
- W1566137581 hasConcept C7301908 @default.
- W1566137581 hasConcept C86803240 @default.
- W1566137581 hasConcept C95444343 @default.
- W1566137581 hasConceptScore W1566137581C110121322 @default.
- W1566137581 hasConceptScore W1566137581C12554922 @default.
- W1566137581 hasConceptScore W1566137581C134306372 @default.
- W1566137581 hasConceptScore W1566137581C185592680 @default.
- W1566137581 hasConceptScore W1566137581C33923547 @default.
- W1566137581 hasConceptScore W1566137581C55493867 @default.
- W1566137581 hasConceptScore W1566137581C7301908 @default.
- W1566137581 hasConceptScore W1566137581C86803240 @default.
- W1566137581 hasConceptScore W1566137581C95444343 @default.
- W1566137581 hasIssue "8" @default.
- W1566137581 hasLocation W15661375811 @default.
- W1566137581 hasOpenAccess W1566137581 @default.
- W1566137581 hasPrimaryLocation W15661375811 @default.
- W1566137581 hasRelatedWork W131143553 @default.
- W1566137581 hasRelatedWork W1796857384 @default.
- W1566137581 hasRelatedWork W1967838982 @default.
- W1566137581 hasRelatedWork W2034990527 @default.
- W1566137581 hasRelatedWork W2068377508 @default.
- W1566137581 hasRelatedWork W2069024662 @default.
- W1566137581 hasRelatedWork W2122581177 @default.
- W1566137581 hasRelatedWork W2126711826 @default.
- W1566137581 hasRelatedWork W2408420206 @default.
- W1566137581 hasRelatedWork W295592732 @default.
- W1566137581 hasVolume "260" @default.
- W1566137581 isParatext "false" @default.
- W1566137581 isRetracted "false" @default.
- W1566137581 magId "1566137581" @default.
- W1566137581 workType "article" @default.