The Antigenic Nature of Heat‐Treated Human Plasma Protein Fractions

As determined in rabbits, the in vivo plasma survival, i.e. half-life (t½), of albumin produced by the cold-ethanol procedure did not differ significantly from that of native albumin (p>0.5). Plasma survivals of reprocessed and heat-ethanol produced albumins were significantly less than that of the native protein (0.02 < p < 0.05). Chemicallymodified albumin had a considerably reduced t½ (p< 0.001) and was the only albumin shown to be antigenically different from the native protein. Variations in t½s of albumin preparations could not be attributed to differences in their polymer contents.

Section: (3)mentioning

confidence: 99%

Catabolic Half-Lives and Antigenic Relationships of Native, Altered and Commercially Prepared Human Albumins in Rabbits

Anhorn¹,

Sheldon²,

Laschinger³

et al. 1982

“…Some preparations exposed to the same heating procedure did not exhibit the new antigen, indicating that heating alone did not produce the new antigen. Lundblad et al [1] showed that human plasma protein fractions (88% albumin, 8% a-globulin and 4% /?-globulin) heated for 10 h at 60 °C were free of any antigen foreign to human serum and were nonreactive and nonantigenic when used clinically. Wolberg et al [4] determined that aggregates of mildly denatured albu min had antigenic determinants which were not found in native or dena tured unaggregated bovine albumin.…”

Section: Maurer and Subrahmanyammentioning

confidence: 99%

Detection of an Antigen in Albumin Subjected to Repeated Heating

Cohen¹,

Roelands²

1976

Stabilized 5 and 25% normal serum albumin (human) derived from plasma, placentas and plasma-placental blends was subjected to repeated heating at 56 °C for 120 h, interspersed with storage at 4 °C for 48 h. Immunoelectrophoretic analyses showed that after the ninth heating, 5% plasma albumin developed a component which migrated in the α-globulin region and gave a reaction of nonidentity with albumin. This antigen, which was not detected in the other albumin samples, reacted with antiserum prepared against control 5% plasma albumin, indicating that it was present in the latter at an undetectably low concentration.

“…We considered it important to test for the presence of foreign antigens in the pro duct as these have previously been reported in products of heat fractionation [14].…”

Section: Safetymentioning

confidence: 99%

Ethanol and Heath-Treated Plasma Fractionation Methods in South Africa

Villiers¹,

Wilson²

1978

Modifications of the Cohn techniques are the methods of choice for the preparation of dilute albumin (PPS) and ϒglobulin solutions on an industrial scale. For the manufacture of refined albumin solutions, however, considerable labour and material is saved if crude, ethanol-precipitated fractions are heated in the presence of stabilisers in order to purify the albumin. The technique is simple and cheap, and yields a safe product of high quality. Bacterially contaminated and highly haemoglobinized plasma can be successfully heat-treated.