Search PubMed⌕ Search

Biomedical subjects

E Karlsson

Publications and source records attributed to E Karlsson.

At least 109 records · Page 6Linked to original sources
PubMed1983

An attempt to identify amino groups of Naja naja siamensis neurotoxin that interact with acetylcholine receptor by a comparison of their reactivities in free and receptor-bound neurotoxin.

An attempt to identify amino groups of Naja naja siamensis neurotoxin that interact with acetylcholine receptor by a comparison of their reactivities in free and receptor bound neurotoxin. Toxicon 21, 219-229, 1983--Free Naja naja siamensis neurotoxin was acetylated with non-radioactive and acetylcholine receptor-bound neurotoxin with radioactive acetic anhydride. The toxins from the two experiments were combined and the monoacetyl derivatives isolated by chromatography on Bio-Rex 70. The yields were determined by spectrophotometry and scintillation counting. To localize the acetyl group, a radioactive monoacetyl toxin was oxidized with performic acid, digested with trypsin and a peptide with the radioactive acetyl group was isolated by gel filtration on Sephadex G-25 and high voltage paper electrophoresis. Amino acid analysis indicated from which part of the molecule the peptide was derived. In free toxin, Ac-Lys 23 and 49 account for 56% and 12%, respectively, of the monoacetyl derivatives, and in bound toxin for only 25% and 8%. Lys 49 is as reactive as Ile 1 in free toxin and 50-150% more reactive than Lys 69, 35 and 12, but it has the lowest reactivity in bound toxin, being only about half as reactive as any of these three residues. The large decrease in reactivity of Lys 23 and 49 indicates that they interact with the receptor. The proximity of the receptor makes them less accessible to acetic anhydride. The reactivities are compared to that of Lys 12, which in free toxin has the least reactive amino group. The yield of Ac-Lys 23 relative to that of Ac-Lys 12 drops from 12.4 to 1.5, or by 88%, Lys 49, 2.6 and 0.5 (81%); Ac-Ile 1, 2.6 and 1.1 (58%); Ac-Lys 69, 1.9 and 0.9 (53%); Ac-Lys 35, 1.8 and 1.0 (44%). The drop in reactivity relative to that of Lys 12 indicates a real decrease, provided that Lys 12 does not become more reactive in bound toxin. This is unlikely, since sequence homology shows that Lys 12 corresponds to Lys 15 of the neurotoxin oxiana II of Naja naja oxiana, a residue known to interact with the receptor. Sequence homology also supports the conclusion that the drop in the reactivity of Ile 1 has the same cause. The receptor-binding region of the siamensis toxin is rather large, containing the residue Lys 23 and 49, Ile 1 and probably also Lys 69 and 35.

Acetylation↗
PubMed1983

Hygiene for the newborn--to bath or to wash?

Appropriate skin care of newborns is performed partly to prevent infection but also for aesthetic and cleansing purposes. Skin care should involve cleansing with a non-toxic, non-abrasive neutral material. This study compared the relative risks and benefits of washing versus bathing with regard to bacterial colonization rate, clinical infection rate, body temperature and crying. The results confirm our clinical impression that bathing and washing routines do not differ with regard to signs of infection or other clinical complications. However, the washing routine does increase the babies heat loss and make them less comfortable.

Bacterial Infections↗
PubMed1983

Proteolytic-independent cobra neurotoxin inhibiting activity of Curcuma sp. (Zingiberaceae).

The 1: 1 (w/v) aqueous extract of Curcuma sp. (Zingiberaceae) was shown to antagonize the toxic action of Naja naja siamensis neurotoxin possibly via direct inactivation of the toxin. The plant extract possessed proteolytic activity which could be separated from the neurotoxin inhibiting activity. The mechanism of antagonism between the plant extract and the neurotoxin was shown not to be involved with the existence of proteolytic activity in the plant extract.

Animals↗
PubMed1983

[Study of long-chain neurotoxins from Naja naja siamensis and Naja naja oxiana venoms by circular dichroism and fluorescence].

CD and fluorescence spectroscopy were used to study the conformational mobility of long-chain neurotoxins from the venom of cobra Naja naja siamensis and Naja naja oxiana (STX and NT-I, respectively). Microenvironment of tryptophan residues in these neurotoxins and their lysine-modified derivatives was also analyzed. Ionization of His22 (pK 5,4-5,6) in STX influences the invariant Trp29 microenvironment. No conformational change was observed on titration of single His residue situated in the C-terminal part of NT-I. Attachment of dansyl groups at Lys39 or Lys60 residues in NT-I is without effect on the native neurotoxin conformation. The distances from these labels to Trp29 or Trp33 indole rings are no shorter than 1,0 nm. The data obtained for STX and NT-I indicate that the STX X-ray structure may serve as a basis for studies on the solution conformation of the long-chain neurotoxins.

Amino Acid Sequence↗
PubMed1982

Effects of purified cardiotoxins from the Thailand cobra (Naja naja siamensis) on isolated skeletal and cardiac muscle preparations.

Four polypeptides were isolated by non-exchange chromatography from the crude cardiotoxin fraction of Thailand cobra (Naja naja siamensis) venom. Fraction I and 71 amino acid residues including 1 tryptophan, while fractions, II, III and IV had 60 amino acids and no tryptophan. When tested on isolated skeletal muscle (chick biventer cervicis, chick embryo muscle in culture, guinea pig hemidiaphragm) and cardiac muscle (guinea pig and cat left atria, cat papillary muscle) preparations, fractions II, III and IV, but not fraction I, caused contracture and depolarization. The cardiotoxin-induced contractions could be prevented by pretreatment with raised concentrations of calcium, but were not influenced by a wide range of pharmacological agents which modify nerve-muscle transmission or muscle contractility. The results suggest that cardiotoxins do not act at a specific step in normal excitation-contraction coupling but directly on cell membranes, where they probably cause the formation of pores which result in depolarization and in the influx of calcium.

Amino Acids↗
PubMed1982

Interaction surfaces of neurotoxins and acetylcholine receptor.

Binding of neurotoxin II Naja naja oxiana derivatives containing one spin label at various positions (Leu 1, Glu 2, Lys 15, Lys 25, Lys 26, His 31, Lys 44 and Lys 46) to purified solubilized acetylcholine receptor protein (AchR) from Torpedo marmorata was studied by EPR techniques. AchR interaction with several dansylated neurotoxin II derivatives was followed by difference fluorescence spectroscopy. A series of neurotoxin II p-azidobenzoyl derivatives were prepared and in three of them modified lysine residues were identified. In combination, spectroscopic data and photolabeling implicate a considerable area of the neurotoxin in association with AchR. Rigidity of the neurotoxin II conformation allowed to regard its binding surface as a mould of the AchR corresponding site and to estimate the minimal size of the latter. Conformation of the long-chain neurotoxins and their binding to AchR are briefly discussed basing on the 1H and 19F NMR studies of neurotoxin I Naja naja oxiana, toxin 3 Naja naja siamensis and its acetylated or trifluoroacetylated derivatives, as well as on Achr interaction with the derivatives spin labeled at Lys 27 and His 71.

Acetylcholine↗
PubMed1982

Protease inhibitor homologues from mamba venoms: facilitation of acetylcholine release and interactions with prejunctional blocking toxins.

1 Five polypeptides, which were isolated from elapid snake venoms and which are structurally related to protease inhibitors, were tested for action on isolated biventer cervicis nerve-muscle preparations of the chick. 2 Dendrotoxin from the Eastern green mamba (Dendroaspis angusticeps) and toxins K and I from the black mamba (Dendroaspis polylepis polylepis) increased to indirect stimulation without affecting responses to exogenous acetylcholine, carbachol of KCl. 3 The two other protease inhibitor homologues, HHV-II from Ringhals cobra (Hemachatus haemachatus) and NNV-II from Cape cobra (Naja nivea) did not increase responses to nerve stimulation. Trypsin inhibitor from bovine pancreas also had no facilitatory effects on neuromuscular transmission. 4 The facilitatory toxins from mamba venoms interacted with the prejunctional blocking toxins, beta-bungarotoxin, crotoxin and notexin, but not with taipoxin. The blocking effects of beta-bungarotoxin were reduced by pretreatment with the mamba toxins, whereas the blocking actions of crotoxin and notexin were enhanced. 5 The results indicate that protease inhibitor homologues from mamba venoms form a new class of neurotoxin, which acts to increase the release of acetylcholine in response to motor nerve stimulation. 6 From the interaction studies it is concluded that the facilitatory toxins bind to motor nerve terminals at sites related to those occupied by the prejunctional blocking toxins. However, differences in interactions with individual toxins suggest that there must be several related binding sites on the nerve terminals.

Acetylcholine↗
PubMed1982

The insulin-releasing activity of the tropical plant momordica charantia.

An aqueous extract from the unripe fruits of the tropical plant Momordica charantia was found to be a potent stimulator of insulin release from beta-cell-rich pancreatic islets isolated from obese-hyperglycemic mice. The stimulation of insulin release was partially reversible. It differed from that of D-glucose and other commonly employed insulin secretagogues in not being suppressed by L-epinephrine and in even being potentiated by the removal of Ca2+. This anomalous behaviour was not associated with general effects on the metabolism of the beta-cells as indicated by an unaltered oxidation of D-glucose. Studies of 45Ca fluxes suggest that the insulin-releasing action is the result of perturbations of membrane functions. In support for the idea of direct effects on membrane lipids, the action of the extract was found to mimic that of saponin in inhibiting the Ca2+/H+ exchange mediated by the ionophore A23187 in isolated chromaffin granules and release Ca2+ from preloaded liposomes.

Animals↗