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Biomedical subjects

E P Kang

Publications and source records attributed to E P Kang.

12 recordsLinked to original sources
PubMed1980

An improved thaw-siphon method for the cryoprecipitate preparation.

Cryoprecipitates were prepared by various techniques including slow-thaw, rapid-thaw, thaw-centrifuge and thaw-siphon methods. Recoveries of 42.3 +/- 9.5% for slow-thaw, 48.8 +/- 8.8% for rapid-thaw, 41.3 +/- 15.8% for thaw-centrifuge and 67.4 +/- 8.9% for thaw-siphon in factor VIII activity were obtained. These results indicated that cryoprecipitate prepared by the thaw-siphon method had the best recovery of the factor VIII procoagulant activity. However, the final volume of the plasma was rather difficult to control and there was a risk that some factor-VIII-containing materials were siphoned with the cryo-poor plasma, especially approaching the end of the process. A modified thaw-siphon method was developed which involved stopping the siphon after 60 min, centrifuging and expressing the remaining plasma to a final volume of less than 15 ml. A yield of 67.1 +/- 9.8% factor VIII activity was obtained. This product is similar to that produced by the original thaw-siphon method in yield but about half in volume.

Chemical Precipitation↗
PubMed1977

Fibrin digestion by thrombin. Comparison with plasmin-digested fibrinogen.

Solutions of plasminogen-free human fibrinogen alone or (1) treated with sodium p-chloromercuribenzoate in order to inactivate factor XIII, or (2) enriched with factor XIII, cysteine and CaC12, were clotted with plasmin-free human thrombin and incubated under sterile conditions. The clots dissolved gradually within 2 days (fibrin from sodium p-chloromercuribenzoate-treated fibrinogen) to 15 days (fibrin from factor XIII-enriched fibrinogen). This proteolytic process was not affected by soybean trypsin inhibitor but was completely inhibited by hirudin. Gel electrophoresis of the thrombin digests indicated the formation of bands equivalent to bands X, Y, D and E of plasmin digests of fibrinogen. The two latter bands, whose identity was confirmed by immunoelectrophoresis, appeared at a more advanced stage of proteolysis than the corresponding bands of plasmin digests. The number of isopeptide bonds present did not appear to affect the rate of release of acid-soluble peptides. Gel electrophoresis and the rate of release of acid-soluble peptides indicated that fewer bonds are hydrolysed by thrombin at the time of the complete solubilization of the clot than are split by plasmin when fibrinogen becomes unclottable by thrombin.

Blood Coagulation↗