The Concentrations of Retinol-Binding Protein, Prealbumin, and Transferrin in the Sera of Newly Delivered Mothers and Children of Various Ages

Vahlquist, Anders; Rask, Lars; Peterson, Per A.; Berg, T.

doi:10.1080/00365517509095782

Cited by 39 publications

(30 citation statements)

References 22 publications

(8 reference statements)

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“…Prealbumin is a rapidly synthesized protein with a biologic half-life of 48 h (25) and considered to be a negative acute phase reactant. The concentrations of prealbumin and transferrin in plasma in all infants in this study were within the normal levels for the age group (20,28). These findings suggest adequate protein nutrition in all infants.…”

Section: Discussionsupporting

confidence: 52%

Formula with Reduced Protein Content: Effects on Growth and Protein Metabolism during Weaning

1988

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ABSTRACT. A total of 20 healthy term infants between 4 and 6 months of age were randomly assigned to either a low protein formula (F1.3) containing 1.3 g protein/100 ml or a high protein formula (F1.8) containing 1.8 g protein/ 100 ml. Both formulas were isocaloric (72 kca1/100 ml) and had a whey-casein ratio of 50:50. Ten control infants were breast-fed (BF). The mean protein intakes (including supplementary foods) were 1.9 + 0.3,2.6 + 0.2, and 1.3 f 0.2 g/kg/day, respectively. The mean concentrations of serum urea were 2.8 + 0.6 (F1.3), 4.1 + 0.6 (F1.8), and 2.2 f 0.8 mmol/liter (BF) at 6 months (F1.3 versus BF, NS, F1.8 versus BF, p < 0.001). The urine excretion of nitrogen was similar in the F1.3 and BF groups being 81 and 78 mg/kg/day. In the Fl.&group nitrogen excretion was higher, 138 mg/kg/day. Plasma concentrations of albumin, prealbumin, and transferrin were normal and similar in the groups. Weight gain was significantly higher in the F1.8 group, 22.8 + 1.7 g/kg/wk when compared to the F1.3 and BF groups, 19.9 +: 3.9 and 18.0 + 4.3 (p < 0.01), respectively. These data indicate that a decreased proteinintake from formula during weaning results in many indices of protein metabolism and growth more similar to those found in BF infants than when conventional follow-up formulas are used. (Pediatr Res 24: 297-301, 1988) Abbreviations F1.8, high protein formula F1.3, low protein formula BF, breast-fed

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Section: Discussionsupporting

confidence: 52%

Formula with Reduced Protein Content: Effects on Growth and Protein Metabolism during Weaning

1988

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“…No distinct difference of amino acid composition between H2 and A2 was also observed (Table 1). Taken together with both clinical (23) and experimental studies (24,25) on the renal handling of RBP, these findings strongly suggest that the molecular species of rabbit urinary RBP are originated from a common plasma holo-RBP, presumably identical with the H2 species obtained from the urine.…”

Section: Species Of Rabbit Rbp 281mentioning

confidence: 76%

“…In any event, the present study on the molecular species of rabbit urinary RBP strongly suggests that major component in glomerular filtrate is holo-RBP, in particular H2 species, which will be derived from a small, but metabolically active pool of uncomplexed RBP in the plasma (25). The possibility of specific change(s) in primary structure of RBP (i.e.…”

Section: Species Of Rabbit Rbp 281mentioning

confidence: 99%

Partial characterization of molecular species of retinol-binding protein found in tubular proteinuria due to chronic cadmium poisoning in the rabbit.

Nakanishi

Muto

1976

Journal of Nutritional Science and Vitaminology, J Nutr Sci Vit

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SummaryA study was conducted to characterize the molecular species of retinol-binding protein (RBP) isolated from the urine of rabbits chronically poisoned with cadmium. The RBP species , identical with regard to both molecular size (approximately 20,000) and immuno reactivity, were separated into four fractions by means of polyacrylamide gel electrophoresis (PAGE), which yielded two holo-RBP (H2 and Hl) and two apo-RBP (A2 and A1) species. The urinary excretion ratio of these fractions (H2:Hi:A2:Al) was found to be about 70:6:21:3 . No distinct difference of amino acid composition between holo-and apo-RBP was observed. An additional species of apo-RBP (designated An) was also isolated from the aged holo-RBP (H2) by isoelectric focusing in gel. Using the separated molecular species of rabbit RBP as well as of human RBP, their interactions with human prealbumin (PA) were examined both by human PA-Sepharose affinity chromatography, and by gel filtration on Sephadex G-100 after in vitro incubation of the RBP with human PA. Purified rabbit holo-RBP exhibited almost the same bind ing ability to human PA as did human RBP. Retinol within RBP molecule enhanced the affinity to PA, presumably through the change of tertiary structure, although the presence of retinol was not essential for the protein-protein interaction.

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“…The concentrations of RBP and prealbu min observed in rhesus mother, fetus and amniotic fluid vary significantly (table I); a similar pattern is observed in man [8,9,[11][12][13]. For this reason, specific activities (dpm/pg protein) were investigated.…”

Section: Discussionmentioning

confidence: 99%

Vitamin A Transfer to the Fetus and to the Amniotic Fluid in Rhesus Monkey <i>(Macaca mulatto)</i>

Vahlquist

Nilsson

1984

Ann Nutr Metab

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The mechanisms of the fetal transmission of vitamin A were investigated by injecting ¹²⁵I-retinol-binding protein (RBP), ¹³¹I-prealbumin and ³H-retinol-RBP in 9 pregnant rhesus monkeys. Samples of blood, amniotic fluid, and when needed fetal liver and kidney were collected after 2.5–48 h. ¹²⁵I-RBP and ¹³¹I-prealbumin were detected in fetal plasma and amniotic fluid already in the first samplings. The specific radioactivity of fetal RBP increased during the first 25 h but never exceeded 13% of the maternal value. This is presumably due to concurrent synthesis of RBP (and prealbumin) by the fetus. The maximum specific activity of ¹²⁵I-RBP in amniotic fluid was 70% of the maternal value indicating that the protein was predominantly derived from the mother. ³H-retinol was more readily transmitted to fetal plasma than RBP. A significant portion of the ³H activity was found in the lipoproteins suggesting that some retinol enters the fetal circulation by other routes than those involving transmission of RBP. The high specific activity of retinol in the fetal kidney implicates its direct involvement in the turnover of transmitted vitamin A. Quantitatively, however, the accumulation of vitamin A activity was largest in the fetal liver.

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The Concentrations of Retinol-Binding Protein, Prealbumin, and Transferrin in the Sera of Newly Delivered Mothers and Children of Various Ages

Cited by 39 publications

References 22 publications

Formula with Reduced Protein Content: Effects on Growth and Protein Metabolism during Weaning

Formula with Reduced Protein Content: Effects on Growth and Protein Metabolism during Weaning

Partial characterization of molecular species of retinol-binding protein found in tubular proteinuria due to chronic cadmium poisoning in the rabbit.

Vitamin A Transfer to the Fetus and to the Amniotic Fluid in Rhesus Monkey <i>(Macaca mulatto)</i>

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