Bovine adrenal medullary granules isolated by millipore filtration were depleted of CA and ATP by dialysis. The resulting material showed an ability to bind inorganic cations and biogenic amines in a concentration-dependent manner. The similarity of the uptake curves, the identical uptake maxima and the narrow pH range (between 4-7) over which the uptake of the inorganic and organic cations took place indicated a binding of these ions to common sites. In addition, the fact that all the uptake curves fitted the Rothmund-Kornfeld equation for cation exchangers corroborated the cation exchanger properties of the dialyzed granule material. The CA binding capacity corresponded to 20-30% of the normal CA content of bovine medullary granules.
Studies on the uptake and storage of sodium and biogenic amines (phenylethylamine, noradrenaline, histamine) by two weak cation-exchangers, IRC-50 and Sephadex C-50, and by biogenic granule-enriched preparations demonstrated that the synthetic and biogenic materials had several common characteristics. They showed similar concentration- and pH-dependence and fitted the same cation-exchange and receptor-binding equations. The observations were taken to support the view that the matrices of amine-storing granules have the properties of weak cation-exchangers, with carboxyls as the cation-binding groups.
Protamine and heparin form a water‐insoluble complex (PHC) at pH 7. This complex has the ability to bind sodium, histamine and monoamines electrostatically. Titrations have suggested the PHC to be formed by a linkage between the guanidino groups of the protamine and the sulphuric acid and most of the carboxylic acid groups of the heparin. The cationic binding properties of the PHC may be assigned to the terminal COO group of the protamine poly‐peptide chain. The qualitative similarities in the cationic binding properties of the PHC and rat mast cell granules are discussed, with special reference to the mechanism of histamine storage in the mast cell granules.
Mast cell granules free of a surrounding membrane were isolated from water-lysed rat peritoneal and thoracic mast cells by differential centrifugation. The granules were depleted of their histamine by suspension in 10 mM sodium phosphate buffer and the sodium-charged granules then converted into the "hydrogen form" by repeated washing in slightly acid deionized water. The cation exchanger properties of the mast cell granules were investigated by testing the applicability of the Rothmund-Kornfeld equation for cation exchangers to the binding of Na+ and Hi+ ions to granule sites. The results lend further support to the view that the mast cell granule acts as a cation exchanger with the exchanger function localized to protein carboxyls in the protein-heparin complex of the granule matrix.
The synthetic carboxylic cation exchanger resin Amberlite IRC-50 was charged with histamine by suspension in histamine-containing solution with admixture of [14C]histamine. Mast cell granules were isolated from mast cells suspended in isotonic sucrose. The release of histamine induced from the two materials by superfusion with isotonic NaCl and KCL solutions showed identical kinetics, in accordance with the view that the release of histamine is due to a cation exchange: Na+ (K+) in equilibrium Hi+ at carboxyl groups in the granule heparin-protein complex.
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