The Effects of Radiation on the Stability of Radio-iodinated Human Serum Albumin

Bloom, H. J. G.; Crockett, David J.; Stewart, F. S.

doi:10.1259/0007-1285-31-367-377

Cited by 9 publications

(4 citation statements)

References 6 publications

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“…Iodination of the purified proteins was accomplished with lZ5I or 1311 (Amersham, England) using the iodine monochloride technique of McFarlane [16] as outlined earlier [17]. Sterile human albumin (kindly supplied by Kabi AB, Stockholm) or plasma was added to prevent damage of the labelled proteins due to self-irradiation [18]. Subsequently, the preparations were subjected to chromatography on freshly prepared, autoclaved Sephadex G-200 in sterile PBS at f4'C.…”

Section: Preparation Of Labelled Proteinmentioning

confidence: 99%

Metabolism of the Vitamin A Transporting Protein Complex

Vahlquist

Peterson

Wibell

1973

Eur J Clin Investigation

134

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Abstract. Biological turnover studies of the human vitamin A transporting protein complex and its individual components, prealbumin and retinol binding protein (RBP) have been performed in normal persons and in patients with severely impaired kidney function. The metabolic behaviour of prealbumin was very similar in the two groups of subjects studied, and it was concluded that prealbumin eatabolism can be dependent to only a minor extent on normally functioning kidney glomeruli.–RBP is present in several molecular forms in plasma. In normal conditions virtually all PRB is bound to prealbumin, but small amounts of RBP also occur in free form. The concentration of the free RBP is greatly increased in patients with grossly impaired glomerular filtration. The biological half‐life for free RBP was short in normal persons (about 4 hours) whereas in the patients this parameter was increased 10 to 15 fold. These findings suggest that most if not all free RBP in plasma is catabolized by the kidney. RBP complexed with prealbumin has a considerably longer half‐life than its free counterpart in normal persons but the absolute synthetic rate of the two components of RBP is similar. Thus it is proposed that most RBP is catabolized from the pool of the uneomplexed species.–From the data it can be calculated that as much as one third of the plasma vitamin A may be deposited in the kidney tubuli on degradation of RBP, since the mechanism for the renal eatabolism of this small protein seems to involve glomerular filtration followed by tubular reabsorption.

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Section: Preparation Of Labelled Proteinmentioning

confidence: 99%

Metabolism of the Vitamin A Transporting Protein Complex

Vahlquist

Peterson

Wibell

1973

Eur J Clin Investigation

134

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“…Because of its possible denaturing effect (34)(35)(36), heat treatment after separation of the albumin was specifically avoided. The albumin was lightly iodinated by the best method available to this laboratory, and the levels of radiation to which the albumin was exposed were well below those known to cause radiation damage to protein (33,37,38). Both testing by physicochemical methods and appraisal of in vivo behavior were used to assess the degree to which isolation and iodination had denatured the albumin.…”

Section: General Assumptionsmentioning

confidence: 99%

Studies of I131-Albumin Catabolism and Distribution in Normal Young Male Adults*

Beeken¹,

Volwiler²,

Goldsworthy³

et al. 1962

J. Clin. Invest.

134

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“…Accepted 18 January 1982 criticized by several authors, who demonstrated the presence of labile fractions in their preparations, caused by self-irradiation damage (Bloom, Crockett & Stewart, 1958;Freeman, 1959;Yalow & Berson, 1957), although at present most of these problems have been surmounted. The use of high molecular weight dextrans for plasma volume determinations has been advocated (Wasserman & Mayerson, 1955;Semple, 1956;Craig & Waterhouse, 1957;Jaenike, Schreiner & Waterhouse, 1957).…”

Section: Discussionmentioning

confidence: 99%

Plasma volume determination by use of enzyme dilution in the dog

et al. 1982

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The use of enzymes for plasma volume determination in the dog was investigated. Plasma volume was determined from dilution of intravenously injected enzymes and compared with results obtained by high molecular weight fluorescein-labelled dextran. Aspartate aminotransferase and alanine aminotransferase from liver tissue gave good results, but the activities of creatine kinase and lactate dehydrogenase from heart tissue were inhibited in plasma, resulting in an overestimation of plasma volume. Enzymes offer a useful alternative to methods presently used since no radioactive isotopes are needed. In laboratory animals the enzyme preparations are readily obtainable and there is minimal risk of immunological complications arising after repeated determinations.

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The Effects of Radiation on the Stability of Radio-iodinated Human Serum Albumin

Cited by 9 publications

References 6 publications

Metabolism of the Vitamin A Transporting Protein Complex

Metabolism of the Vitamin A Transporting Protein Complex

Studies of I131-Albumin Catabolism and Distribution in Normal Young Male Adults*

Plasma volume determination by use of enzyme dilution in the dog

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