Über die Vehikelfunktion der Serumeiweißkörper

Bennhold, H.

doi:10.1007/978-3-642-90641-1_5

Cited by 67 publications

(24 citation statements)

References 103 publications

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“…Since all of the bilirubin in serum is protein-bound (11,14,(26)(27)(28) and that in urine protein-free (11), it is probable that excretion occurs predominantly by way of the tubules rather than by glomerular filtration (34). The most perplexing problem is the relationship of the urinary excretion of bilirubin to its concentration in blood.…”

Section: Commentmentioning

confidence: 99%

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The Significance of the “One-Minute” (Prompt Direct Reacting) Bilirubin in Serum 1

Klatskin¹,

Drill²

1950

J. Clin. Invest.

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Section: Commentmentioning

confidence: 99%

“…The failure to demonstrate unbound bilirubin in serum by dialysis (25), cataphoresis (14,(26)(27)(28) or ultrafiltration (10,11,14) casts doubt on the theory that the type of van (29). Gray and Whidborne (9) suggest that the direct reaction may be due to the presence of a catalyst in serum specifically elaborated in regurgitation jaundice.…”

mentioning

confidence: 99%

The Significance of the “One-Minute” (Prompt Direct Reacting) Bilirubin in Serum 1

Klatskin¹,

Drill²

1950

J. Clin. Invest.

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“…It has the remarkable capacity to enter into combination with many molecules and ions in a manner different from other proteins (8). This property also has made albumin a valuable supplement to a medium for the growth of tubercle bacilli (9).…”

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confidence: 99%

The Use of Concentrated Human Serum Albumin in the Treatment of Cirrhosis of the Liver 1

Kunkel¹,

Labby²,

Ahrens³

et al. 1948

J. Clin. Invest.

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The formation of ascites in patients with cirrhosis of the liver probably depends on at least three factors: (1) hypoalbuminemia, (2) portal hypertension, and (3) increased amounts of circulating antidiuretic substance. The relative importance of these factors varies with the individual patients. Although the formation and disappearance of ascites do not correlate perfectly with levels of serum albumin in all patients, in the majority of cases the two findings are coincident and apparently related (1, 2). The use of concentrated human serum albumin in these patients for its osmotic effect would be expected to cause a diuresis. The extent to which this diuresis is produced would depend in large part upon the relative importance of the various factors of ascites production, being most marked in those patients in whom hypoalbuminemia is most specifically at fault.The observations of Janeway (3) and Thorn (4) and their co-workers in patients with liver disease demonstrated that the albumin level of the serum could be raised to normal by repeated injections of albumin. Certain of their patients showed a loss of edema and ascites but the oncotic effects were disappointing in their experience.

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“…The affinity of serum albumin to various chemical dyes and to bilirubin has been observed previously (32,33,11) and further investigations of the binding capacities of the various serum components will prove very instructive. In mixtures of Hp and isolated proteins such as egg albumin, globulin gamma, or Felton solution, however, the Hp migrates independently and can be entirely dissociated from the proteins, if runs are continued sufficiently long.…”

Section: Discussionmentioning

confidence: 66%

Studies on Photo-Oxidation of Antigen and Antibodies

Smetana

Shemin

1941

Journal of Experimental Medicine

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1. Quantitative precipitin studies indicate that progressive photo-oxidation progressively destroys the antigenic function of egg albumin. 2. Quantitative precipitin reactions of antisera (anti-egg albumin rabbit serum and antipneumococcus Type I horse serum) demonstrate that progressive photo-oxidation causes progressive lowering of the potency of the sera. 3. Quantitative precipitin reactions of the photo-oxidized globulin gamma fraction of anti-egg albumin rabbit serum and of Felton solution of antipneumococcus Type I horse serum show that these specific antibody fractions behave similarly to antibodies in whole sera. 4. Egg albumin whose precipitin reaction is destroyed by photo-oxidation no longer causes anaphylaxis in guinea pigs and does not produce precipitins in rabbits. 5. Chemical studies of progressively photo-oxidized egg albumin show a progressive destruction of tryptophane and histidine while tyrosine remains intact and cystine is reversibly oxidized. Sulfhydryl groups can no longer be demonstrated in photo-oxidized egg albumin whose antigenic characteristics are greatly weakened. 6. Similar studies on the globulin gamma fraction of anti-egg albumin rabbit serum and on Felton solution show no diminution of these amino acids in photo-oxidized material whose antigenic properties are destroyed. 7. The non-coagulable nitrogen and the amino nitrogen of egg albumin, antisera, and their specific antibody fractions show but an insignificant increase during photo-oxidation, indicating that the loss of the precipitin reaction is not due to splitting of the respective protein molecules. 8. Electrophoretic studies of egg albumin, antisera, and their specific antibody fractions show that photo-oxidation causes a marked alteration of the pattern of these substrates. 9. Photo-oxidation of proteins causes the formation of aggregates, indicating denaturation. 10. Hematoporphyrin migrates with the albumin fraction of unaltered as well as the photo-oxidized anti-egg albumin rabbit serum and pneumococcus Type I horse serum; in isolated proteins such as egg albumin, globulin gamma, or Felton solution, etc., the dye moves independently of the protein; after progressive photo-oxidation Hp becomes progressively fixed to the protein. Eosin behaves similarly to hematoporphyrin.

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Über die Vehikelfunktion der Serumeiweißkörper

Cited by 67 publications

References 103 publications

The Significance of the “One-Minute” (Prompt Direct Reacting) Bilirubin in Serum 1

The Significance of the “One-Minute” (Prompt Direct Reacting) Bilirubin in Serum 1

The Use of Concentrated Human Serum Albumin in the Treatment of Cirrhosis of the Liver 1

Studies on Photo-Oxidation of Antigen and Antibodies

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