FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1489224259> ?p ?o ?g. }

• W1489224259 endingPage "18259" @default.
• W1489224259 startingPage "18247" @default.
• W1489224259 abstract "Abstract The primary structure of the two major isoforms (alpha and gamma) of troponin C (TnC) from crayfish tail muscle has been determined by the application of manual and automated Edman degradation procedures to fragments generated by suitable chemical and proteolytic cleavages. Both amino acid sequences commence with an acetylated methionyl residue and contain 150 amino acid residues, including a single proline residue at position 29 and 2 residues of tyrosine at positions 95 and 102. No cysteine or tryptophan are present. The molecular weights calculated for alpha- and gamma-TnC are 17,157 and 16,974, respectively. The two crayfish proteins are invariable at 129 positions and conserved at 11 others. Pairwise comparisons show that the two sequences are 33-39% identical with those of seven TnCs reported so far and 39% identical with that of bovine brain calmodulin. The N-terminal end of about 10 residues, found in vertebrate TnCs, is absent in crayfish TnCs. In the latter proteins, domains I and III appear as abortive Ca2+-binding sites due to nonconservative amino acid replacements at the key Ca2+-coordinating positions in their loops. The remaining two Ca2+-binding loops (II and IV) show a remarkable similarity with the Ca2+-specific loops (I and II) found in vertebrate TnCs. These findings are consistent with the Ca2+-binding data (Wnuk, W. (1989) J. Biol. Chem. 264, 18240-18246) which indicate the presence of two Ca2+-specific sites in crayfish TnCs. These two sites display the same affinity for Ca2+ (log KCa = 4.3) on gamma-TnC but differ in their affinity (log KCa = 6.0 and 4.1) on alpha-TnC. The only structural difference between the dodecapeptide loops II and IV in both alpha- and gamma-TnC, which correlates with the existence of the high affinity (log KCa = 6.0) Ca2+-specific site on alpha-TnC, is position 11 occupied by a methionyl residue in the loop IV of alpha-TnC as opposed to negatively charged residues found in the other three loops. This suggests that the high affinity Ca2+-specific site on alpha-TnC is located in domain IV. Since the Ca2+-binding studies show that the formation of the complex of crayfish troponin I (TnI) with alpha- and gamma-TnC increases significantly the affinity of only one of their two Ca2+-specific sites and this TnI-sensitive site is not the high affinity Ca2+-specific site on alpha-TnC, we conclude that the binding of Ca2+ to site II controls the Ca2+-dependent interaction between crayfish TnCs and TnI." @default.
• W1489224259 created "2016-06-24" @default.
• W1489224259 creator A5028337407 @default.
• W1489224259 creator A5032974967 @default.
• W1489224259 creator A5083515989 @default.
• W1489224259 creator A5088523323 @default.
• W1489224259 date "1989-10-01" @default.
• W1489224259 modified "2023-10-12" @default.
• W1489224259 title "Amino acid sequences of the two major isoforms of troponin C from crayfish" @default.
• W1489224259 cites W1232330100 @default.
• W1489224259 cites W1469833000 @default.
• W1489224259 cites W1524101826 @default.
• W1489224259 cites W1550330933 @default.
• W1489224259 cites W1567044991 @default.
• W1489224259 cites W1578284467 @default.
• W1489224259 cites W1587627399 @default.
• W1489224259 cites W1589370248 @default.
• W1489224259 cites W1598771652 @default.
• W1489224259 cites W1601860320 @default.
• W1489224259 cites W1605459033 @default.
• W1489224259 cites W1848560850 @default.
• W1489224259 cites W1885844626 @default.
• W1489224259 cites W1966902394 @default.
• W1489224259 cites W1985476834 @default.
• W1489224259 cites W1986196445 @default.
• W1489224259 cites W1990502944 @default.
• W1489224259 cites W1991891293 @default.
• W1489224259 cites W1993423515 @default.
• W1489224259 cites W2013260039 @default.
• W1489224259 cites W2022114235 @default.
• W1489224259 cites W2037710668 @default.
• W1489224259 cites W2040389590 @default.
• W1489224259 cites W2068294014 @default.
• W1489224259 cites W2073883999 @default.
• W1489224259 cites W2088255441 @default.
• W1489224259 cites W2095450147 @default.
• W1489224259 cites W2113079144 @default.
• W1489224259 cites W2210986612 @default.
• W1489224259 cites W2315065987 @default.
• W1489224259 cites W4235081531 @default.
• W1489224259 cites W4251627122 @default.
• W1489224259 doi "https://doi.org/10.1016/s0021-9258(19)84704-x" @default.
• W1489224259 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2681191" @default.
• W1489224259 hasPublicationYear "1989" @default.
• W1489224259 type Work @default.
• W1489224259 sameAs 1489224259 @default.
• W1489224259 citedByCount "48" @default.
• W1489224259 countsByYear W14892242592013 @default.
• W1489224259 countsByYear W14892242592014 @default.
• W1489224259 crossrefType "journal-article" @default.
• W1489224259 hasAuthorship W1489224259A5028337407 @default.
• W1489224259 hasAuthorship W1489224259A5032974967 @default.
• W1489224259 hasAuthorship W1489224259A5083515989 @default.
• W1489224259 hasAuthorship W1489224259A5088523323 @default.
• W1489224259 hasBestOaLocation W14892242591 @default.
• W1489224259 hasConcept C104317684 @default.
• W1489224259 hasConcept C126322002 @default.
• W1489224259 hasConcept C133927893 @default.
• W1489224259 hasConcept C185592680 @default.
• W1489224259 hasConcept C18903297 @default.
• W1489224259 hasConcept C2781403440 @default.
• W1489224259 hasConcept C36036425 @default.
• W1489224259 hasConcept C500558357 @default.
• W1489224259 hasConcept C515207424 @default.
• W1489224259 hasConcept C53345823 @default.
• W1489224259 hasConcept C55493867 @default.
• W1489224259 hasConcept C71924100 @default.
• W1489224259 hasConcept C86803240 @default.
• W1489224259 hasConcept C90856448 @default.
• W1489224259 hasConceptScore W1489224259C104317684 @default.
• W1489224259 hasConceptScore W1489224259C126322002 @default.
• W1489224259 hasConceptScore W1489224259C133927893 @default.
• W1489224259 hasConceptScore W1489224259C185592680 @default.
• W1489224259 hasConceptScore W1489224259C18903297 @default.
• W1489224259 hasConceptScore W1489224259C2781403440 @default.
• W1489224259 hasConceptScore W1489224259C36036425 @default.
• W1489224259 hasConceptScore W1489224259C500558357 @default.
• W1489224259 hasConceptScore W1489224259C515207424 @default.
• W1489224259 hasConceptScore W1489224259C53345823 @default.
• W1489224259 hasConceptScore W1489224259C55493867 @default.
• W1489224259 hasConceptScore W1489224259C71924100 @default.
• W1489224259 hasConceptScore W1489224259C86803240 @default.
• W1489224259 hasConceptScore W1489224259C90856448 @default.
• W1489224259 hasIssue "30" @default.
• W1489224259 hasLocation W14892242591 @default.
• W1489224259 hasOpenAccess W1489224259 @default.
• W1489224259 hasPrimaryLocation W14892242591 @default.
• W1489224259 hasRelatedWork W1534305969 @default.
• W1489224259 hasRelatedWork W1983903437 @default.
• W1489224259 hasRelatedWork W2058525629 @default.
• W1489224259 hasRelatedWork W2063814210 @default.
• W1489224259 hasRelatedWork W2069154979 @default.
• W1489224259 hasRelatedWork W2120759692 @default.
• W1489224259 hasRelatedWork W2147093254 @default.
• W1489224259 hasRelatedWork W2318386800 @default.
• W1489224259 hasRelatedWork W2552415159 @default.
• W1489224259 hasRelatedWork W4242263026 @default.
• W1489224259 hasVolume "264" @default.

• next