Oviparity in a Sea-Snake (Laticauda colubrina)

Nature ◽  
1930 ◽  
Vol 126 (3174) ◽  
pp. 312-313 ◽  
Author(s):  
NORMAN SMEDLEY
Keyword(s):  
Sea Snake ◽  
Laticauda Colubrina

Neuromuscular effects of a toxic phospholipase A2 and its nontoxic homologue from the venom of the sea snake, Laticauda colubrina

Toxicon ◽  
1989 ◽  
Vol 27 (5) ◽  
pp. 587-591 ◽  
Author(s):  
Edward G. Rowan ◽  
Alan L. Harvey ◽  
Chikahisa Takasaki ◽  
Nobuo Tamiya
Keyword(s):  
Phospholipase A2 ◽  
Sea Snake ◽  
Laticauda Colubrina

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.

Observations on the habits and morphology of the sea snake Laticauda colubrina (Schneider) in Fiji

1977 ◽  
Vol 55 (10) ◽  
pp. 1612-1619 ◽  
Author(s):  
J. C. Pernetta
Keyword(s):  
Sexual Dimorphism ◽  
Colour Pattern ◽  
Morphometric Characters ◽  
Sea Snake ◽  
Reproductive Characteristics ◽  
Black And White ◽  
Fiji Islands ◽  
Laticauda Colubrina

Fifty specimens of Laticauda colubrina were collected from two localities in the Fiji Islands and variation in a number of nonmetric and morphometric characters recorded. Marked sexual dimorphism is apparent in all characters examined. Details of the habits, diet (reef eels), and reproductive characteristics of this species are given. The function of the black and white banded colour pattern is discussed, and the validity of the currently recognized species of Laticauda is examined.

Blood respiratory properties in a sea snake and a land snake

1976 ◽  
Vol 24 (3) ◽  
pp. 313 ◽  
Author(s):  
RS Seymore
Keyword(s):  
Oxygen Transport ◽  
Buffer Capacity ◽  
Haemoglobin Concentration ◽  
Oxygen Affinity ◽  
Sea Snake ◽  
Plasma Bicarbonate ◽  
Sea Snakes ◽  
Oxygen Capacity ◽  
Snake Blood ◽  
Laticauda Colubrina

Haematocrit, haemoglobin concentration, oxygen capacity, haemoglobin-oxygen affinity (Hb-O2) and buffer capacity of whole blood are examined in the banded sea snake, Laticauda colubrina, and the terrestrial black snake, Pseudechis porphyriacus, two ecologically divergent, but phylogenetically close, species. Oxygen capacity is indistinguishable between both snakes and, in general, there is no distinct trend toward high values in diving reptiles. Hb-O2 affinity is slightly higher in the sea snake. The Bohr effect is smaller in sea snake blood but haem-haem interaction is similar in both species. However, it is proposed that moderate differences in the Bohr shift and haem-haem interaction are of little importance to oxygen transport in most reptiles. Plasma bicarbonate is moderately high in both snakes and there is no difference in non-carbonic buffer capacity. In general, the respiratory properties of the blood of sea snakes are not greatly different from those of terrestrial snakes and lizards.

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