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najas flexilis/tyrosine
Veza se sprema u međuspremnik
15 rezultatima
Effects of modification of tyrosines 3 and 62 (63) on enzymatic and toxicological properties of phospholipases A2 from Naja nigricollis and Naja naja atra snake venoms.
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Previously we selectively modified His (48), Arg, Lys, Asp, Glu and Trp residues in the basic phospholipase A2 from Naja nigricollis and the acidic phospholipase A2 from N. n. atra snake venoms. Evidence was obtained for the existence of separate but perhaps overlapping sites responsible,
Effect of modification of tyrosine residues in cytotoxin-1 from Indian cobra venom. (Naja naja naja).
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The role of tyrosine residues in the biological activity of cytotoxin-1 was evaluated using N-bromo succinimide. N-bromo succinimide effected the oxidation of tyrosine residues in cytotoxin-1 with an increase in absorption at 260 nm. N-chloro succinimide was ineffective in the oxidation of tyrosine
Role of tyrosine and tryptophan residues in the structure-activity relationships of a cardiotoxin from Naja nigricollis venom.
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This paper is an attempt to localize the critical area determining toxicity in a snake cardiotoxin. Toxin gamma is a single-chain polypeptide of 60 amino acids, which has been isolated from the venom of the African spitting cobra, Naja nigricollis. Three aromatic residues, namely, Trp-11, Tyr-22,
[The effect of the venom on the central Asian cobra Naja naja oxiana on tyrosine-C-14 incorporation in the cellular structures of mouse liver].
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Chemical modification of tyrosine residue in "toxin B" from the venom of the Indian cobra, Naja naja.
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The complete covalent structure of a cardiotoxin from the venom of Naja nigricollis (African black-necked spitting cobra).
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The complete covalent structure of a small, basic protein with cardiotoxic activity is described. This has been isolated from the venom of Naja nigricollis by gel filtration on Sephadex G-75 and gradient ion exchange chromatography on Bio-Rex 70. The cardiotoxin, molecular weight 6806 from amino
Immunochemical properties of Naja naja atra (Taiwan cobra) phospholipase A2 using polyclonal and monoclonal antibodies.
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The immuno-chemical properties of Naja naja atra phospholipase A2 (NNA-PLA2) were studied by using the chemically modified PLA2 derivatives and the PLA2 homologues toward anti-NNA-PLA2 polyclonal and monoclonal antibodies. Anti-NNA-PLA2 polyclonal antibodies inhibited the enzymatic activity of
Structure and chemical modifications of neurotoxin from Naja nigricollis studied by Raman spectroscopy.
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Raman spectroscopy was used to determine structural features of the native toxin alpha from Naja nigricollis, which contains only one Trp and one Tyr, and of chemically modified toxins having chromophores added to these two conserved aromatic amino acids. The percentages of secondary structure were
Chemical modification of the histidine residue in phospholipase A2 (Naja naja naja). A case of half-site reactivity.
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Reaction of phospholipase A2 (Naja naja naja) with p-bromophenacyl bromidine leads to almost complete loss of enzymatic activity. The rate of inactivation is pH-dependent with pKa equals 6.9 for the ionizing residue. p-Bromophenacyl bromide modifies 0.5 mol of histidine/mol of enzyme as judged by
L-amino acid oxidase from Naja atra venom activates and binds to human platelets.
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An L-amino acid oxidase (LAAO), NA-LAAO, was purified from the venom of Naja atra. Its N-terminal sequence shows great similarity with LAAOs from other snake venoms. NA-LAAO dose-dependently induced aggregation of washed human platelets. However, it had no activity on platelets in platelet-rich
Proton-nuclear-magnetic-resonance study of the conformation of neurotoxin II from Middle-Asian cobra (Naja naja oxiana) venom.
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A proton nuclear magnetic resonance (NMR) study at 100 and 300 MHz of neurotoxin II from the venom of Middle-Asian cobra Naja naja oxiana has been performed in 2H2O and H2O solutions. By means of chemical modification and double resonance all the aromatic residue resonances have been assigned. From
Characterization of mocarhagin, a cobra venom metalloproteinase from Naja mocambique mocambique, and related proteins from other Elapidae venoms.
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Mocarhagin, a cobra venom metalloproteinase from Naja mocambique mocambique, has previously been shown to cleave selectively two mucin-like substrates on platelets and neutrophils within anionic amino acid sequences containing sulfated tyrosines. We now show that purified mocarhagin has
The oxidation of methionine and its effect of the properties of cardiotoxin VII1 from Naja melanoleuca venom.
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Methionine residues 24 and 26 of cardiotoxin VII1 from Naja melanoleuca were oxidised to sulphoxides using N-chlorosuccinimide at pH 8.5. The number of equivalents of oxidant required for complete oxidation suggested that the methionine side-chains existed in a relatively "exposed" conformational
Purification and characterization of a myotoxic phospholipase A2 from Indian cobra (Naja naja naja) venom.
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A major phospholipase A2 (NN-XIII-PLA2) which constitutes 20% of the whole Naja naja naja venom was purified to homogeneity on CM-Sephadex C-25 column chromatography. NN-XIII-PLA2 is a basic protein with a mol. wt of 11,200 by SDS-PAGE. This enzyme has low enzymatic activity but is more toxic to
Purification and properties of the L-amino acid oxidase from monocellate cobra (Naja naja kaouthia) venom.
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1. The L-amino acid oxidase of the monocellate cobra (Naja naja kaouthia) venom was purified to electrophoretic homogeneity. The molecular weight of the enzyme was 112,200 as determined by Sephadex G-200 gel filtration chromatography, and 57,400 as determined by SDS-polyacrylamide gel
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