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D J Kok

Publications and source records attributed to D J Kok.

75 records · Page 5Linked to original sources

Excessive crystal agglomeration with low citrate excretion in recurrent stone-formers.

In 7 highly recurrent calcium oxalate stone-formers and 10 healthy subjects the effects of urine on three processes of calcium oxalate monohydrate crystallisation--solubility, crystal growth, and crystal agglomeration--were studied. The urine of the stone-formers showed low calcium oxalate solubility and normal crystal growth inhibition, but lacked the ability to inhibit crystal agglomeration. As the sole metabolic abnormality, all stone-formers showed hypocitraturia. Normalisation of urinary citrate concentration resulted both in vitro and in vivo in a significant rise in agglomeration inhibition. These results show that inhibition of agglomeration is a very important, probably citrate-regulated, process in calcium oxalate stone formation.

Adult↗

Regulation of the C3 nephritic factor stabilized C3/C5 convertase of complement by purified human erythrocyte C3b receptor.

Activation of complement may result in the generation of the amplification convertase C3bBb. This convertase can be stabilized by properdin (P) or C3NeF. C3bBbP is susceptible to inactivation by beta 1H, while C3bBbNeF is relatively resistant. Since it has been shown that the human erythrocyte C3b receptor (CR1) is able to inactivate C3bBbP, the inactivating action of CR1 on C3bBbNeF was investigated CR1 is at least five times more efficient than beta 1H in inactivating C3bBbNeF. Kinetic studies revealed that CR1 induces an enhanced biphasic kinetics of decay of C3bBbNeF; further purification of this C3NeF preparation by cation exchange chromatography showed that this phenomenon is dependent on the population of C3NeF. Finally CR1 is also able to inactivate fluid phase C3bBbNeF.

Complement Activating Enzymes↗