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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 265 (1970), S. 442-454 
    ISSN: 1432-1912
    Keywords: Haemolysis ; Phospholipase A ; Direct Lytic Factor ; Polypeptides ; Toxins ; HÄmolyse ; Phospholipase A ; Direkt lytischer Faktor ; Polypeptide ; Toxine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The haemolytic action on washed guinea-pig red cells of the following substances has been studied: the direct lytic factor (DLF) of cobra venom, melittin and an apamin-containing fraction of bee venom, anaphylatoxin (AT), angiotensin, vasopressin, saponin, p-chloro-mercuribenzoate (p-CMB) and N-ethylmaleimide (NEM). Further the synergism of these substances with phospholipase A in causing haemolysis has been investigated. In regard to the lytic effects, the substances studied can be classified as follows. 1. Substances which react with SH-groups, either by means of -S-S- bonds (DLF, apamin-fraction, AT, vasopressin) or by other structures (p-CMB, NEM) produce weak or no direct haemolysis, but strongly potentiate haemolysis caused by phospholipase A. Their effect is increased by Ca++, inhibited by EDTA, and strongly dependent on temperature (as far as has been investigated). 2. Angiotensin, a peptide without disulfide groups, is not haemolytic, neither directly nor in combination with phospholipase A. Saponin, which does not react with SH-groups, also does not show potentiated haemolysis with phospholipase A in spite of being haemolytic itself. 3. Melittin, though not containing disulfide structures, does produce potentiated haemolysis with phospholipase A, even at concentrations which are not lytic when acting alone. It is concluded that more than one mechanism of potentiating phospholipase A haemolysis exists. One possibility is the reaction of potentiating agents with SH-groups of membrane constituents (enzymes?) of the red cells. This mechanism applies to p-CMB, NEM and to disulfide-containing peptides. It is independent of detergent effects. Another mechanism may be membrane changes due to a lowering of surface tension such as that produced by melittin. It seems doubtful, however, whether this is the only molecular property responsible for the potentiation, as the detergent saponin does not have such an effect. Possibly melittin, in addition to having detergent effects interferes with the same membrane properties which are altered by the SH-reactants.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 266 (1970), S. 199-207 
    ISSN: 1432-1912
    Keywords: Prostaglandin ; Phospholipase A ; Arachidonic Acid ; Acetylcholine ; Frog Intestine ; Prostaglandin ; Phospholipase A ; Arachidonsäure ; Acetylcholin ; Froschdarm
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary 1. Frog intestines were perfused through their vascular system and the content of prostaglandin (PG) in the effluent was estimated biologically. 2. The spontaneous release of PG ranged from 0.55 to 29 ng PGE1 equivalents/min. Thin-layer chromatography indicated that the liberated compound was a PGE compound. 3. Acetylcholine and dimethyl-phenyl-piperazinium iodide raised the output of PG significantly. Adrenaline had no definite effect. 4. Lysolecithin weakly stimulated the release of PG, but phospholipase A caused an extraordinary rise which was apparently due to formation of new PGE1. 5. A considerable formation of PG was also seen when arachidonic acid was infused. Being PGE2 it obviously originated from the infused fatty acid. This fact demonstrates directly that a PG-forming enzyme system is active in the intact tissue. 6. It is suggested that physiological stimuli can increase the formation of PG by providing free precursor acids. This could be effected by the activation of an endogenous phospholipase A.
    Type of Medium: Electronic Resource
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