scholarly journals The disulphide bonds of erabutoxin a, a neurotoxic protein of a sea-snake (Laticauda semifasciata) venom

1971 ◽  
Vol 122 (4) ◽  
pp. 463-467 ◽  
Author(s):  
Y. Endo ◽  
S. Sato ◽  
S. Ishii ◽  
N. Tamiya
Keyword(s):  
Amino Acid ◽  
Sulphuric Acid ◽  
Column Chromatography ◽  
Paper Electrophoresis ◽  
Sea Snake ◽  
Toxin Molecule ◽  
Disulphide Bonds ◽  
N Terminus ◽  
Laticauda Semifasciata

Erabutoxin a was partially hydrolysed with enzymes and sulphuric acid and the resulting peptides were separated from each other by column chromatography and paper electrophoresis. From the results of amino acid analyses of the sulphur-containing peptides and their oxidized components, all four disulphide bridges in the toxin molecule were located. The disulphide bonds were found between half-cystine residues at positions 3 and 24, 17 and 41, 43 and 54, and 55 and 60 from the N-terminus.

scholarly journals The neurotoxins of the sea snake Laticauda schistorhynchus

1983 ◽  
Vol 213 (1) ◽  
pp. 39-41 ◽  
Author(s):  
M L Guinea ◽  
N Tamiya ◽  
H G Cogger
Keyword(s):  
Amino Acid ◽  
Electrophoretic Mobility ◽  
Column Chromatography ◽  
Amino Acid Analysis ◽  
Sea Snake ◽  
Laticauda Semifasciata ◽  
Cellulose Column

Erabutoxins a and b, the major neurotoxins in the venom of the sea snake Laticauda semifasciata, were detected in the venom of Laticauda schistorhynchus. The identity of the toxins was confirmed on the basis of elution position on CM-cellulose column chromatography, disc electrophoretic mobility, amino acid analysis and toxicity measurement.

scholarly journals The amino acid sequences of erabutoxins, neurotoxic proteins of sea-snake (Laticauda semifasciata) venom

1971 ◽  
Vol 122 (4) ◽  
pp. 453-461 ◽  
Author(s):  
S. Sato ◽  
N. Tamiya
Keyword(s):  
Amino Acid ◽  
Paper Electrophoresis ◽  
Amino Acid Sequences ◽  
Edman Degradation ◽  
Terminal Sequence ◽  
Amino Acid Sequence Analysis ◽  
Sea Snake ◽  
Tryptic Digest ◽  
Laticauda Semifasciata ◽  
Erabutoxin B

1. Erabutoxin b was reduced, S-carboxymethylated and hydrolysed with trypsin. Seven tryptic fragments were isolated by column chromatography and paper electrophoresis. Some of the fragments were further hydrolysed with α-chymotrypsin, pepsin, Nagarse, Proctase A or Proctase B. The amino acid sequences of the fragment peptides were determined by subtractive Edman degradation. 2. From the tryptic digest of reduced, S-carboxymethylated and trifluoroacetylated erabutoxin b two fragments were isolated. From the amino acid composition of the fragments and from the terminal sequence studies on the reduced and S-carboxymethylated erabutoxin b, the sequence of the above seven tryptic fragments was elucidated. 3. The tryptic digestion of reduced and S-carboxymethylated erabutoxin a gave fragments, only one of which was different from the corresponding fragment from erabutoxin b. The amino acid sequence analysis of the fragment peptide showed that the only difference between erabutoxins a and b was that the former had asparagine and the latter had histidine at position 26.

scholarly journals The isolation, properties and amino acid sequence of erabutoxin c, a minor neurotoxic component of the venom of a sea snake Laticauda semifasciata

1972 ◽  
Vol 130 (2) ◽  
pp. 547-555 ◽  
Author(s):  
N. Tamiya ◽  
H. Abe
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Gel Filtration ◽  
Disc Electrophoresis ◽  
Amino Acid Residues ◽  
Sea Snake ◽  
Acetylcholine Contracture ◽  
Laticauda Semifasciata ◽  
A Minor ◽  
Erabutoxin B

Erabutoxin c, a minor neurotoxic component of the venom of a sea snake Laticauda semifasciata, was isolated in pure form by repeated column chromatography on CM-cellulose columns. The toxin was crystallizable and monodisperse in rechromatography, disc electrophoresis and isoelectric focusing (isoelectric point, pH9.23–9.25). The molecular weight of the toxin, as estimated by gel filtration, was 7000. The toxin showed the same lethal activity to mice (0.13μg/g body wt., intramuscular injection) and the same effect on isolated frog muscle as erabutoxins a and b, the main toxic components of the venom. The toxin inhibited the acetylcholine contracture but not the potassium chloride contracture of muscle. Erabutoxin c consisted of 62 amino acid residues, containing one fewer lysine and one more histidine than erabutoxin a and one fewer lysine and one more aspartic acid (or asparagine) than erabutoxin b. Erabutoxin c was reduced, S-carboxymethylated and hydrolysed with trypsin. The only fragment different from the corresponding fragments from erabutoxin b was hydrolysed further with pepsin. One of the peptic fragments, which was assumed to have the aspartic acid (or asparagine) residue in question at the C-terminal end, was treated with carboxypeptidase A. The C-terminal residue was found to be an asparagine. It was therefore concluded that erabutoxin c was [51-asparagine]-erabutoxin b.

scholarly journals Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases

1986 ◽  
Vol 234 (2) ◽  
pp. 429-434 ◽  
Author(s):  
G Salvesen ◽  
C Parkes ◽  
M Abrahamson ◽  
A Grubb ◽  
A J Barrett
Keyword(s):  
Amino Acid ◽  
Inhibitory Activity ◽  
Cathepsin L ◽  
Limited Proteolysis ◽  
Cysteine Proteinases ◽  
Disulphide Bonds ◽  
N Terminus ◽  
Domain 3 ◽  
The Individual ◽  
Activity Domain

We point out that human low-Mr kininogen contains three cystatin-like sequences, rather than two, as had previously been thought. The protein was purified by affinity chromatography on carboxymethyl-papain-Sepharose, and subjected to limited proteolysis by trypsin and chymotrypsin. Fragments were isolated, and three corresponding to the individual cystatin-like domains were identified. By comparison with the known amino acid sequence of the protein they were numbered 1 to 3 from the N-terminus. Domain 1 was not found to have any inhibitory activity for cysteine proteinases, which is consistent with the absence of residues that are highly conserved in inhibitors of the cystatin superfamily, and have previously been suggested to be essential for activity. Domain 2 was a good inhibitor of chicken calpain, and also papain and cathepsin L. Domain 3 showed negligible inhibition of calpain, but inhibited papain and cathepsin L strongly. The probable arrangement of disulphide bonds in the heavy chain of low-Mr kininogen is deduced from the homology with the cystatins and other evidence contained in the present paper.

Correction of amino acid sequence of phospholipase A2 I from the venom of Laticauda semifasciata (erabu sea snake)

Toxicon ◽  
1988 ◽  
Vol 26 (8) ◽  
pp. 747-749 ◽  
Author(s):  
Chikahisa Takasaki ◽  
Hiromi Kuramochi ◽  
Tsuneo Shimazu ◽  
Nobuo Tamiya
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Phospholipase A2 ◽  
Sea Snake ◽  
Laticauda Semifasciata

scholarly journals The primary structure of the toxin Laticauda semifasciata III, a weak and reversibly acting neurotoxin from the venom of a sea snake, Laticauda semifasciata

1974 ◽  
Vol 141 (2) ◽  
pp. 389-400 ◽  
Author(s):  
Nobuyo Maeda ◽  
Nobuo Tamiya
Keyword(s):  
Amino Acid ◽  
Primary Structure ◽  
Amino Acid Residues ◽  
Sea Snake ◽  
Sea Snakes ◽  
Laticauda Semifasciata

A weak and reversibly acting neurotoxic protein of Laticauda semifasciata venom, Laticauda semifasciata III (component LsIII), was sequenced. Component LsIII consists of 66 amino acid residues and has five disulphide bridges, one of which was located between residues 26 and 30. The weak and reversible neurotoxicity of component LsIII is discussed in relation to its structure, which falls between those of the neuro- and cardiotoxins of sea snakes and Elapidae snakes isolated and sequenced so far.

scholarly journals Correction of the amino acid sequences of erabutoxins from the venom of the sea snake Laticauda semifasciata

1985 ◽  
Vol 226 (3) ◽  
pp. 879-880 ◽  
Author(s):  
S Nishida ◽  
Y Kokubun ◽  
N Tamiya
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Sea Snake ◽  
Laticauda Semifasciata

The amino acid sequences of erabutoxins a and b were reinvestigated. The previously reported sequences of Gln-His at positions 6 and 7, and of Pro-Ser at positions 18 and 19 of erabutoxins a and b were corrected to His-Gln and Ser-Pro respectively.

scholarly journals Amino acid sequences of three phospholipases A I, III and IV from the venom of the sea snake Laticauda semifasciata

1982 ◽  
Vol 207 (3) ◽  
pp. 589-594 ◽  
Author(s):  
S Nishida ◽  
H S Kim ◽  
N Tamiya
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Phospholipase A ◽  
Tryptophan Residue ◽  
British Library ◽  
Amino Acid Residues ◽  
Single Chain ◽  
Sea Snake ◽  
Laticauda Semifasciata ◽  
Phospholipases A

Amino acid sequences of three phospholipases A, I, III and IV, from the venom of the sea snake Laticauda semifasciata were elucidated. Each protein consisted of a single chain of 118 amino acid residues, including 14 half-cystine residues. They showed high homology among themselves, and with the other snake-venom phospholipases A and with the enzymes from mammalian pancreas. Phospholipases A III and IV were especially similar to each other, with only four differences out of their 118 amino acid residues. Phospholipase A I contained one tryptophan residue at position 64, which was important for enzymic activity, whereas III and IV did not contain tryptophan residues and their corresponding positions were occupied by leucine residues. The substitution by leucine resulted in a decreased, but definite, phospholipase A activity. The substituted enzymes have a more potent neuromuscular blocking activity. Full experimental details and evidence for the amino acid sequences of the proteins have been deposited as Supplementary Publication SUP 50118 (39 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J.(1981)193,5.

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