Effects of Repeated Heating on Human Albumin<sup>1</sup>

Roelands, Joan F.; Moody, Michael; Cohen, Pinya

doi:10.1111/j.1423-0410.1974.tb02716.x

Cited by 11 publications

(13 citation statements)

References 17 publications

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“…The appearance of the new precipitin arc following the ninth heating is in agreement with our earlier report [3] of a peak in the a-globulin region on cellulose acetate electrophoresis which increased in 5% plasma albumin samples throughout the nine heatings. There was only a slight increase in this peak upon repeated heating of 5% placental or plasmaplacental blends of albumin, and by immunoelectrophoresis there were no additional precipitin arcs in the a-globulin region.…”

Section: Maurer and Subrahmanyamsupporting

confidence: 80%

“…Of the three at each protein concentration, there was one lot each fractionated from plasma, placentas, and a blend of these sources. Antisera were produced to these albumins, which had been com mercially heated for only 10 h at 60 °C, and to the same samples after they had been subjected in our laboratory to as many as nine additional heatings at 56 ± 1 °C for 120 h. Following each heating, the samples were refrigerated for 2 days at 4 °C [3]. New Zealand, female rabbits approx imately 2-3 kg were immunized subcutaneously with 25 mg of albumin in complete Freund's adjuvant (Difco).…”

Section: Maurer and Subrahmanyammentioning

confidence: 99%

“…They suggested that conformational changes related to aggregation were implicated in the emergence of new determinants. We have reported on physicochemical changes occurring in stabilized human serum albumin subjected to repeated heatings [3]. The…”

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confidence: 99%

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Detection of an Antigen in Albumin Subjected to Repeated Heating

Cohen¹,

Roelands²

1976

Vox Sanguinis

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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.

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Section: Maurer and Subrahmanyamsupporting

confidence: 80%

Section: Maurer and Subrahmanyammentioning

confidence: 99%

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Detection of an Antigen in Albumin Subjected to Repeated Heating

Cohen¹,

Roelands²

1976

Vox Sanguinis

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“…Other investigators have reported that increases in the concentration of a compo nent with the electrophoretic properties of a-globulin occurred when NSA [13], plasma [19], or serum [20] was heated. Mackay and Martin [21] found that a component with lower net charge than albumin was formed when purified human albumin was held at 58 °C for 6 h in 0.15MNaCl, pH 6.8 with little or no stabilizer.…”

Section: Discussionmentioning

confidence: 99%

“…The composition of 5% protein solutions was deter mined by cellulose acetate membrane electrophoresis (CAE) as described previously [13], Samples were electrophoresed for 16 min at 250 V in barbital buffer, pH8.6, ionic strength 0.075. Membranes were stained with PonceauS and quantitated by densitometry.…”

Section: Cellulose Acetate Membrane Electrophoresismentioning

confidence: 99%

Stabilization of Human Albumin by Caprylate and Acetyltryptophanate

Yu¹,

Finlayson²

1984

Vox Sanguinis

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The thermal stabilization of human albumin by caprylate (CA) and acetyltryptophanate (AT) was studied by monitoring the formation of albumin polymer (defined as species larger than dimer) on the basis of its molecular size as well as its characteristic migration as α-globulin. Heating 5% protein solutions of purified albumin monomer, Cohn fraction V, and fraction IV-4 + V at 60°C in 0.1 M sodium phosphate or 145 mM sodium chloride, pH 7.0, established the following order of stabilizer effectiveness: 4 mM CA + 4mM AT ≈ 4 mM CA>8 mM AT≥2mM CA>4 mM AT. However, albumin was more thermally stable in the chloride medium. Raising the CA concentration above 4 mM provided little additional stabilization. The D- and L-enantiomers of AT were equally effective, but 16 mM AT was needed to equal the effect of 4 mM CA. L-Tryptophanate exerted only slight stabilization, even at 32 mM\ D-tryptophanate was even less effective. The albumin polymer level increased progressively with time at 60 °C in 2 mM CA or 4 mM AT, whereas in 4 mM CA it reached a plateau in 4-6 h. Acetone drying of albumin-rich fractions was shown to remove nearly all endogenous fatty acid, rendering the protein thermally labile unless sufficient exogenous stabilizer(s) was added. Even in the presence of 145 mM sodium chloride and 4 mM CA + 4 mM AT or 4 mM CA, the stabilizing effect of endogenous fatty acid was still detectable.

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