FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2408833597> ?p ?o ?g. }

• W2408833597 endingPage "5026" @default.
• W2408833597 startingPage "5020" @default.
• W2408833597 abstract "Bovine prothrombin has been demonstrated to selfassociate both in the absence and presence of Ca2+ ions. Prothrombin Fragment 1 (residues 1 to 156 of prothrombin) self-associates in the presence of Ca2+ and other divalent cations, but not in their absence. Prethrombin 1 (residues 157 to 582 of prothrombin) selfassociates indistinguishably both in the absence and presence of Ca2+ ions. Self-association of Prothrombin Fragment 1 in the presence of Mn2+ ions has been shown to be dimerization both by sedimentation equilibrium and sedimentation velocity measurements. Association constants for dimerization induced by M&+, Ca”, and Sr2+ ions have been calculated from sedimentation velocity data. The ability of the divalent cations to induce self-association is in the order Mn” >> Ca” 2 Sr2+ > M&+. A hybrid “dime? between prothrombin and Prothrombin Fragment 1 has been demonstrated to form in the presence of Ca2’ ions. Fluorescence polarization studies have demonstrated that the rotational relaxation time for Prothrombin Fragment 1 in a viscous solution is increased approximately a-fold in the presence of Ca’+, implying that self-association is reflected in the spectrally monitored hydrodynamic properties, as well as sedimentation properties of the protein molecule. The tryptic peptide which contains 8 of the 10 y-carboxyglutamic acid residues of prothrombin (residues 12 to 44) binds divalent cations and precipitates, rather than undergoing the limited self-association which occurs with Prothrombin Fragment 1. On the basis of these observations, the self-association behavior of prothrombin must be concluded to occur via at least two different mechanisms, one dependent on the presence of Ca2’ ions and one independent of Ca2+ ions. The following observations suggest that specific, cooperative Ca2+ binding and Ca”-induced selfassociation require particular structural constraints in the protein molecule. 1) Divalent cations induce precipitation of tryptic peptides from prothrombin. 2) Previous results demonstrated that when the disulfide bridges of Prothrombin Fragment 1 were reduced and" @default.
• W2408833597 created "2016-06-24" @default.
• W2408833597 creator A5006790200 @default.
• W2408833597 creator A5012896184 @default.
• W2408833597 creator A5048301059 @default.
• W2408833597 creator A5085193022 @default.
• W2408833597 creator A5085932250 @default.
• W2408833597 date "1979-06-01" @default.
• W2408833597 modified "2023-09-30" @default.
• W2408833597 title "Multiple modes of association in bovine prothrombin and its proteolysis products." @default.
• W2408833597 cites W1129800782 @default.
• W2408833597 cites W1158770474 @default.
• W2408833597 cites W1527880353 @default.
• W2408833597 cites W1531765158 @default.
• W2408833597 cites W1540596657 @default.
• W2408833597 cites W1540769916 @default.
• W2408833597 cites W1566087596 @default.
• W2408833597 cites W1594373951 @default.
• W2408833597 cites W1595472253 @default.
• W2408833597 cites W1603919509 @default.
• W2408833597 cites W181379507 @default.
• W2408833597 cites W1966483504 @default.
• W2408833597 cites W1968406297 @default.
• W2408833597 cites W1973956782 @default.
• W2408833597 cites W1975923363 @default.
• W2408833597 cites W1985111499 @default.
• W2408833597 cites W1987392417 @default.
• W2408833597 cites W1991155431 @default.
• W2408833597 cites W1993442337 @default.
• W2408833597 cites W1995139112 @default.
• W2408833597 cites W2001360032 @default.
• W2408833597 cites W2006764976 @default.
• W2408833597 cites W2012323316 @default.
• W2408833597 cites W2022710224 @default.
• W2408833597 cites W2026268706 @default.
• W2408833597 cites W2027203230 @default.
• W2408833597 cites W2046310917 @default.
• W2408833597 cites W2047216284 @default.
• W2408833597 cites W2053596135 @default.
• W2408833597 cites W2057332998 @default.
• W2408833597 cites W2059217193 @default.
• W2408833597 cites W2061734875 @default.
• W2408833597 cites W2076932299 @default.
• W2408833597 cites W2077739213 @default.
• W2408833597 cites W2083375547 @default.
• W2408833597 cites W2096326108 @default.
• W2408833597 cites W2100837269 @default.
• W2408833597 cites W2111301002 @default.
• W2408833597 cites W2159916641 @default.
• W2408833597 cites W84506637 @default.
• W2408833597 doi "https://doi.org/10.1016/s0021-9258(18)50555-x" @default.
• W2408833597 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/447631" @default.
• W2408833597 hasPublicationYear "1979" @default.
• W2408833597 type Work @default.
• W2408833597 sameAs 2408833597 @default.
• W2408833597 citedByCount "46" @default.
• W2408833597 crossrefType "journal-article" @default.
• W2408833597 hasAuthorship W2408833597A5006790200 @default.
• W2408833597 hasAuthorship W2408833597A5012896184 @default.
• W2408833597 hasAuthorship W2408833597A5048301059 @default.
• W2408833597 hasAuthorship W2408833597A5085193022 @default.
• W2408833597 hasAuthorship W2408833597A5085932250 @default.
• W2408833597 hasBestOaLocation W24088335971 @default.
• W2408833597 hasConcept C181199279 @default.
• W2408833597 hasConcept C185592680 @default.
• W2408833597 hasConcept C2781307694 @default.
• W2408833597 hasConcept C43617362 @default.
• W2408833597 hasConcept C55493867 @default.
• W2408833597 hasConceptScore W2408833597C181199279 @default.
• W2408833597 hasConceptScore W2408833597C185592680 @default.
• W2408833597 hasConceptScore W2408833597C2781307694 @default.
• W2408833597 hasConceptScore W2408833597C43617362 @default.
• W2408833597 hasConceptScore W2408833597C55493867 @default.
• W2408833597 hasIssue "12" @default.
• W2408833597 hasLocation W24088335971 @default.
• W2408833597 hasOpenAccess W2408833597 @default.
• W2408833597 hasPrimaryLocation W24088335971 @default.
• W2408833597 hasRelatedWork W1963486910 @default.
• W2408833597 hasRelatedWork W2006969725 @default.
• W2408833597 hasRelatedWork W2010592006 @default.
• W2408833597 hasRelatedWork W2042283944 @default.
• W2408833597 hasRelatedWork W2092055364 @default.
• W2408833597 hasRelatedWork W2395843297 @default.
• W2408833597 hasRelatedWork W2414415093 @default.
• W2408833597 hasRelatedWork W2441711217 @default.
• W2408833597 hasRelatedWork W2568057209 @default.
• W2408833597 hasRelatedWork W3189468524 @default.
• W2408833597 hasVolume "254" @default.
• W2408833597 isParatext "false" @default.
• W2408833597 isRetracted "false" @default.
• W2408833597 magId "2408833597" @default.
• W2408833597 workType "article" @default.