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 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 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.

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 Amino acid sequences of two novel long-chain neurotoxins from the venom of the sea snake Laticauda colubrina

1982 ◽  
Vol 207 (2) ◽  
pp. 215-223 ◽  
Author(s):  
H S Kim ◽  
N Tamiya
Keyword(s):  
Amino Acid ◽  
Intramuscular Injection ◽  
Solomon Islands ◽  
The Philippines ◽  
Amino Acid Sequences ◽  
Amino Acid Residues ◽  
Sea Snake ◽  
Novel Structure ◽  
Long Chain ◽  
Laticauda Colubrina

From the venom of a population of the sea snake Laticauda colubrina from the Solomon Islands, a neurotoxic component, Laticauda colubrina a (toxin Lc a), was isolated in 16.6% (A280) yield. Similarly, from the venom of a population of L. colubrina from the Philippines, a neurotoxic component, Laticauda colubrina b (toxin Lc b), was obtained in 10.0% (A280) yield. The LD50 values of these toxins were 0.12 microgram/g body wt. on intramuscular injection in mice. Toxins Lc a and Lc b were each composed of molecules containing 69 amino acid residues with eight half-cystine residues. The complete amino acid sequences of these two toxins were elucidated. Toxins Lc a and Lc b are different from each other at five positions of their sequences, namely at positions 31 (Phe/Ser), 32 (Leu/Ile), 33 (Lys/Arg), 50 (Pro/Arg) and 53 (Asp/His) (residues in parentheses give the residues in toxins Lc a and Lc b respectively). Toxins Lc a and Lc b have a novel structure in that they have only four disulphide bridges, although the whole amino acid sequences are homologous to those of other known long-chain neurotoxins. It is remarkable that toxins Lc a and Lc b are not coexistent at the detection error of 6% of the other toxin. Populations of Laticauda colubrina from the Solomon Islands and from the Philippines have either toxin Lc a or toxin Lc b and not both of them.

scholarly journals Isolation, properties and amino acid sequences of a phospholipase A2 and its homologue without activity from the venom of a sea snake, Laticauda colubrina, from the Solomon Islands

1988 ◽  
Vol 253 (3) ◽  
pp. 869-875 ◽  
Author(s):  
C Takasaki ◽  
S Kimura ◽  
Y Kokubun ◽  
N Tamiya
Keyword(s):  
Amino Acid ◽  
Phospholipase A2 ◽  
Solomon Islands ◽  
Amino Acid Sequences ◽  
Molar Ratio ◽  
British Library ◽  
Single Chain ◽  
Sea Snake ◽  
Phospholipase A2 Activity ◽  
Laticauda Colubrina

A phospholipase A2, Laticauda colubrina phospholipase A2 II (LcPLA-II), and a phospholipase A2 homologue, Laticauda colubrina phospholipase A2 homologue I (LcPLH-I), were isolated from the venom of the yellow-lipped sea snake, Laticauda colubrina, from the Solomon Islands. LcPLA-II showed phospholipase A2 activity towards egg-yolk phosphatidylcholine (24 mumol/min per mg at optimal conditions at 37 degrees C) and lethal potency (LD50 45 micrograms/kg body wt. intravenously in mice). Both of the activities were lost by treatment with p-bromophenacyl bromide. LcPLH-I showed neither phospholipase A2 activity nor lethal potency at a dose of 4.5 mg/kg body wt. in mice. It was not modified by the treatment with p-bromophenacyl bromide. LcPLA-II and LcPLH-I bound Ca2+ at a 1:1 molar ratio with KCa values of 105 microM and 44 microM at pH 8.0 respectively. Elucidation of the amino acid sequences of these two proteins showed that each protein consisted of a single chain of 118 amino acid residues, including 14 half-cystine residues. The two sequences are different from each other at 22 residues and highly homologous to those from other sources. The essential histidine residue for the phospholipase A2 activity at position 48 is replaced by an asparagine residue in the homologue LcPLH-I. Details of the separation of the peptides obtained by proteinase digestions of LcPLA-II and LcPLA-I and the determination of their amino acid sequences are given in Supplementary Publication SUP 50145 (14 pages), which has been deposited 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. (1988) 249, 5.

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 Three neurotoxins from the venom of a sea snake Astrotia stokesii, including two long-chain neurotoxic proteins with amidated C-termini

1978 ◽  
Vol 175 (2) ◽  
pp. 507-517 ◽  
Author(s):  
N Maeda ◽  
N Tamiya
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Amide Group ◽  
British Library ◽  
Amino Acid Residues ◽  
Snake Venoms ◽  
Sea Snake ◽  
X Ray ◽  
Almost All ◽  
Long Chain

From the venom of a sea snake Astrotia stokesii three neurotoxic components, toxins Astrotia stokesii a, b and c were isolated in 40, 15 and 5% yield by weight respectively of the whole venom. Their LD50 values for 20g mice were 0.13, 0.096 and 0.098 microgram/g body wt. respectively and accounted for almost all the lethal activity of the venom. Their amino acid sequences were determined. Astrotia stokesii a was composed of 60 amino acid residues with nine half-cystine residues and was quite homologous to other sea-snake short-chain neurotoxins in its amino acid sequence. Toxins Astrotia stokesii b and c were composed of 70 and 72 amino acid residues respectively with 10 half-cystine residues. They are the first long-chain neurotoxins with high activity isolated from sea-snake venoms. The C-terminal carboxy groups of toxins b and c were found to be amidated; the amidation is known for some polypeptides, but is novel for a protein. The amide group may make a hydrogen-bond with glutamic acid-39, which replaces a lysine that has so far been found invariably in long-chain neutrotoxins. Astrotia stokesii b and c are also novel in having phenylalanine-25 and isoleucine- or valine-42. The ordinary Tyr-Glu pair, which is observed in X-ray structure [Low, Preston, Sato, Rosen, Searl, Rudko & Richardson (1976) Proc. Natl. Acad. Sci. U.S.A. 73, 2991-2994] and n.m.r.study [Inagaki, Tatsumi, Miyazawa, Hori & Tamiya (1977) Abstr. Int. Congr. Pure Appl. Chem. 26th, p. 336] on erabutoxins may be replaced by a hydrophobic pair. Detailed evidence for the amino acid sequences of the proteins has been deposited as Supplementary Publication SUP 5009o (30 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7B1, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

Sign in / Sign up

Export Citation Format

Share Document