1,720,978 research outputs found
The hydrolysis of alpha-CBZ-L-lysine-p-nitrophenyl ester by two forms of human urokinase
No full textIdentification of the site of ferrocyanide binding involved in the intramolecular electron transfer process to oxidized heme in Scapharca dimeric hemoglobin.
No full text
The sorcin-annexin VII calcium-dependent interaction requires the sorcin N-terminal domain
No full textSurface plasmon resonance experiments show that at neutral pH the stability of the complex between sorcin and annexin VII (synexin) increases dramatically between 3 and 6 microM calcium; at the latter cation concentration the K(D) value is 0.63 microM. In turn, the lack of complex formation between the sorcin Ca(2+) binding domain (33-198) and synexin maps the annexin binding site to the N-terminal region of the sorcin polypeptide chain. Annexin VII likewise employs the N-terminal domain, more specifically the first 31 amino acids, to interact with sorcin [Brownawell, A.M. and Creutz, C.E. (1997) J. Biol. Chem. 272, 22182-22190]. The interaction may involve similar structural motifs in the two proteins, namely GGYY and GYGG in sorcin and GYPP in synexin
Information transfer in the penta-EF-hand sorcin does not operate vie the canonical structural/functional pairing
No full textMETAL REGULATION OF SIDEROPHORE SYNTHESIS IN PSEUDOMONAS-AERUGINOSA AND FUNCTIONAL-EFFECTS OF SIDEROPHORE-METAL COMPLEXES
No full textSorcin directly influences cardiac Na/Ca exchanger and ryanodine receptor activity via the sorcin C-terminal domain.
No full textINTERACTION OF LACTOFERRIN WITH ESCHERICHIA-COLI-CELLS AND CORRELATION WITH ANTIBACTERIAL ACTIVITY
No full textStructure-function relationships in sorcin, a member of the penta EF-hand family. Interaction of sorcin fragments with the ryanodine receptor and an E.coli model system
No full textA cooperative hemoglobin with directly communicating hemes. The Scapharca inaequivalvis homodimer.
No full text- …
