Effect of Riboflavin Deficiency on the Metabolism of Oxypurines in Chicks

1971 ◽  
Vol 49 (12) ◽  
pp. 1059-1062 ◽  
Author(s):  
S. T. Chou
Keyword(s):  
Uric Acid ◽  
Acid Synthesis ◽  
Xanthine Dehydrogenase ◽  
Broiler Chicks ◽  
Uric Acid Concentration ◽  
Riboflavin Deficiency ◽  
Deficient Diet ◽  
High Incidence ◽  
Liver And Kidney ◽  
Riboflavin Deficient

Day-old broiler chicks of both sexes were used in three experiments to determine the effect of riboflavin deficiency on oxypurine metabolism catalyzed by xanthine dehydrogenase, a riboflavin-containing enzyme. Chicks fed a riboflavin-deficient diet (1.38 mg/kg) for 3 weeks exhibited depressed growth and a high incidence of curled-toe paralysis (higher than 80%) as compared to control chicks (15.1 mg riboflavin per kilogram diet; no incidence of curled-toe paralysis). In addition, the precursors of uric acid, hypoxanthine and/or xanthine, accumulated in the liver and kidney of deficient chicks showing curled-toe paralysis. These observations show that dietary riboflavin being incorporated into xanthine dehydrogenase is essential for oxypurine metabolism. Moreover in the chick, the liver and the kidney may be important sites of uric acid synthesis. The low uric acid concentration in the plasma of the deficient chicks appeared to be indicative of a disturbance in uric acid synthesis in the liver and kidney.

Metabolism of the Black Snake Embryo

1953 ◽  
Vol 30 (4) ◽  
pp. 492-501 ◽  
Author(s):  
HUGH CLARK
Keyword(s):  
Energy Source ◽  
Uric Acid ◽  
Acid Synthesis ◽  
K Value ◽  
Embryonic Tissues ◽  
Hatching Time ◽  
Urea Content ◽  
Foetal Liver ◽  
Liver And Kidney ◽  
Post Deposition

1. Post-deposition growth of the black snake embryo is characterized by k values as follows: days 1-11, 0.46; days 11-34, 0.057; days 34-67, 0.039. 2. Total excreted nitrogen is 12.55 mg. occurring successively in development as ammonia, urea and uric acid; k value of total nitrogen production is 0.062, days 11-67, which in comparison with those of growth during this period suggest that stored protein is an energy source during a large part of development. 3. Urea is excreted into the albumen which is the principal storage reservoir and into the yolk; that which is excreted into the yolk is reabsorbed after the 45th day and re-deposited in the albumen as urea, and is in part (22%) converted to uric acid. 4. Concentration of urea in the yolk and yolk-sac continues to increase at the same rate after the 11th day (k = 0.024), although the actual amount declines after the 45th day; concentration in the embryonic tissues increases to the 58th day, then decreases sharply to hatching time; concentration in the albumen increases throughout development, reaching a concentration of approximately 500 mg.%. 5. Uric acid synthesis is believed to be preceded by urea formation, and the presence of urease in the foetal liver and kidney suggest that the urea is hydrolysed to ammonia which is then incorporated into uric acid. Site of the transformation is uncertain, though the early and persistent localization of uric acid in the chorio-allantoic membrane points to this as the organ of synthesis. Decrease in total urea content is quantitatively identical with increase in uric acid. 6. The significance of these findings in relation to development of the vertebrate cleidoic egg is discussed.

scholarly journals Refection in rats fed on a sucrose-based, riboflavin-deficient diet

1980 ◽  
Vol 43 (1) ◽  
pp. 171-177 ◽  
Author(s):  
A. M. Prentice ◽  
C. J. Bates
Keyword(s):  
Biochemical Tests ◽  
Riboflavin Deficiency ◽  
Deficient Diet ◽  
Biochemical Effects ◽  
Severe Deficiency ◽  
Riboflavin Deficient ◽  
Riboflavin Status

1. Refection, resulting in an increased supply of riboflavin to riboflavin-deficient rats through coprophagy, was demonstrated on a sucrose-based diet when sensitive biochemical tests of riboflavin status were employed: these included measurements of NAD(P)H2:glutathione oxidoreductase (EC 1.6.4.2); succinate:(acceptor) oxidoreductase (EC 1.3.99.1) and NADH:(acceptor) oxidoreductase (EC 1.6.99.3).2. The use of tail-cups to eliminate coprophagy, and hence refection, resulted in a more rapid and reproducible progress into severe deficiency.3. The occurrence of refection on a sucrose-based diet may account for hitherto unexplained differences between previous publications on the biochemical effects of riboflavin deficiency.

scholarly journals Effects of riboflavin deficiency and clofibrate treatment on the five acyl-CoA dehydrogenases in rat liver mitochondria

1988 ◽  
Vol 254 (2) ◽  
pp. 477-481 ◽  
Author(s):  
K Veitch ◽  
J P Draye ◽  
F Van Hoof ◽  
H S A Sherratt
Keyword(s):  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Straight Chain ◽  
Riboflavin Deficiency ◽  
Deficient Diet ◽  
Mitochondrial Fractions ◽  
Chain Acyl ◽  
Branched Chain ◽  
Acyl Coa Dehydrogenases ◽  
Riboflavin Deficient

Rats were maintained on a riboflavin-deficient diet or on a diet containing clofibrate (0.5%, w/w). The activities of the mitochondrial FAD-dependent straight-chain acyl-CoA dehydrogenases (butyryl-CoA, octanoyl-CoA and palmitoyl-CoA) and the branched-chain acyl-CoA dehydrogenases (isovaleryl-CoA and isobutyryl-CoA) involved in the degradation of branched-chain acyl-CoA esters derived from branched-chain amino acids were assayed in liver mitochondrial extracts prepared in the absence and presence of exogenous FAD. These activities were low in livers from riboflavin-deficient rats (11, 28, 16, 6 and less than 2% of controls respectively) when prepared in the absence of exogenous FAD, and were not restored to control values when prepared in 25 microM-FAD (29, 47, 28, 7 and 17%). Clofibrate feeding increased the activities of butyryl-CoA, octanoyl-CoA and palmitoyl-CoA dehydrogenases (by 48, 116 and 98% of controls respectively), but not, by contrast, the activities of isovaleryl-CoA and isobutyryl-CoA dehydrogenases (62 and 102% of controls respectively). The mitochondrial fractions from riboflavin-deficient and from clofibrate-fed rats oxidized palmitoylcarnitine in State 3 at rates of 32 and 163% respectively of those from control rats.

Peripheral Neuropathy Associated with Dietary Riboflavin Deficiency in the Chicken I. Light Microscopic Study

1988 ◽  
Vol 25 (1) ◽  
pp. 9-16 ◽  
Author(s):  
W. D. Johnson ◽  
R. W. Storts
Keyword(s):  
Peripheral Neuropathy ◽  
Schwann Cell ◽  
Cell Swelling ◽  
Riboflavin Deficiency ◽  
Deficient Diet ◽  
Tissue Separation ◽  
Leukocytic Infiltration ◽  
Leg Weakness ◽  
Demyelinating Peripheral Neuropathy ◽  
Riboflavin Deficient

Chickens fed a riboflavin-deficient diet from hatching had leg weakness and paralysis as early as 12 days of age. Signs worsened through day 16; after 35 days, recovery was evident. Sciatic nerves from affected chickens were enlarged. Significant microscopic lesions were confined to peripheral nerves and included tissue separation (suggesting interstitial edema), Schwann cell swelling, perivascular leukocytic infiltration, and segmental demyelination accompanied by accumulation of osmiophilic debris in Schwann cell cytoplasm. Axon degeneration was present, but was not a primary lesion. Acid phosphatase enzyme activity of Schwann cells was increased in affected nerves. These results demonstrate that dietary riboflavin deficiency causes a demyelinating peripheral neuropathy in young, rapidly growing chickens.

STUDIES OF THE MOLECULAR BASIS OF CONGENITAL MALFORMATIONS

PEDIATRICS ◽  
1969 ◽  
Vol 43 (6) ◽  
pp. 915-926
Author(s):  
Bruce Mackler
Keyword(s):  
Congenital Malformations ◽  
Transport Systems ◽  
Congenital Defects ◽  
Synthetic Analog ◽  
Riboflavin Deficiency ◽  
Deficient Diet ◽  
Adult Rats ◽  
Prenatal Environment ◽  
Better Regulation ◽  
Riboflavin Deficient

With recent advances in treatment of many acute and chronic diseases, the problems associated with congenital malformations in children have assumed a greater importance in pediatrics. Previous to the work of Warkany and Nelson in 19401, it was recognized that many congenital defects were genetically determined and hereditary. The finding by Warkany and co-workers1-3 that modification of the prenatal environment by severe states of riboflavin deficiency produced congenital malformations in mammals demonstrated clearly the importance of the prenatal environment in the development of the fetus and gave impetus to searches for other environmental factors of importance to the developing organism. The syndrome resulting from severe maternal riboflavin deficiency in rats is characterized mainly by micrognathia and reduction type of defects in the distal extremities of the fetuses, and by a wide number of other anomalies such as cleft palate and hydronephrosis. More recently, Nelson and co-workers4 demonstrated that galactoflavin, a synthetic analog of riboflavin, produced a rapid riboflavin deficiency syndrome in pregnant rats. The addition of galactoflavin to a riboflavin-deficient diet materially shortened the time required to produce riboflavin deficiency, and permitted much better regulation of the experimental model. In other studies of riboflavin deficiency, Miller and co-workers5 showed a lower flavin content in fetuses from riboflavindeficient rats than in control fetuses, suggesting the possibility that there may be corresponding deficiencies in the activities of flavin-dependent enzymes such as the terminal electron transport systems (ETP). Other investigators6 have reported studies of enzymatic activities in liver mitochondria of adult rats fed a riboflavin-deficient diet with added galactoflavin, but with varying results.

scholarly journals The Anemia of Human Riboflavin Deficiency

Blood ◽  
1965 ◽  
Vol 25 (4) ◽  
pp. 432-442 ◽  
Author(s):  
MONTAGUE LANE ◽  
CLARENCE P. ALFREY
Keyword(s):  
Bone Marrow ◽  
Normocytic Anemia ◽  
Adult Males ◽  
Normal Range ◽  
Riboflavin Deficiency ◽  
Deficient Diet ◽  
Platelet Counts ◽  
Leukocyte Counts ◽  
Riboflavin Deficient

Abstract 1. Riboflavin deficiency was induced in 8 adult males with a riboflavin deficient diet and a riboflavin antagonist, galactoflavin. 2. Each patient developed a normochromic normocytic anemia and reticulocytopenia. 3. The leukocyte counts and platelet counts remained within the normal range throughout the period of deficiency. 4. The bone marrow changes and ferrokinetic characteristics of this anemia have been described. 5. The anemia was reversed by riboflavin administration.

REGULATION OF URIC ACID SYNTHESIS IN EMBRYONIC LIVER AND KIDNEY

1987 ◽  
pp. 397-402
Author(s):  
J. Wittmann ◽  
A. Mengi ◽  
S. Kraußer
Keyword(s):  
Uric Acid ◽  
Acid Synthesis ◽  
Embryonic Liver ◽  
Liver And Kidney

scholarly journals Effect of fasting and of methionine deficiency on L-methionine, DL-methionine and DL-2-hydroxy-4-methylthiobutanoic acid metabolism in broiler chicks

1987 ◽  
Vol 57 (3) ◽  
pp. 429-437 ◽  
Author(s):  
C. Linda Saunderson
Keyword(s):  
Perchloric Acid ◽  
Acid Metabolism ◽  
Broiler Chicks ◽  
Deficient Diet ◽  
C Protein ◽  
Methionine Deficiency ◽  
Liver And Kidney ◽  
Liver Tissues

1. Metabolism of L-[1-14C]methionine, DL-[l-14C]methionine and DL-[ 1-14C]2-hydroxy-4-methylthiobutanoic acid (DL-HMB) by broiler chicks which had been fasted overnight or given a methionine-deficient diet was compared with fed (control) birds.2. The excretion of 14C-labelled material, total 14CO2 exhaled, 14C incorporation into tissue proteins and the 14C-labelled material in perchloric-acid-soluble tissue fractions were measured 6 h after injection of the 14C-labelled materials.3. The incorporation of 14C into tissue proteins and the relative rates of conversion of D-methionine and DL-HMB to L-methionine in tissues under different nutritional regimens were compared using protein-bound 14C:protein-free 14C values.4. Fasted birds exhaled more 14CO2 than control birds but excreted less 14C, while methionine-deficient birds behaved very similarly to the control animals in these respects.5. Fasted birds incorporated much less 14C into proteins of tissues other than liver and kidney from all three labelled tracers. The values for protein-bound 14C: protein-free 14C were lower in all tissues.6. Methionine-deficient birds had similar levels of 14C in tissue proteins but lower values for protein bound 14C: protein-free 14C.7. Examination of the values for protein-bound 14C:protein-free 14C suggest that brain and probably liver tissues from fasted and methionine-deficient birds showed improved rates of conversion of D-methionine and DL-HMB to L-methionine compared with control animals.

Sign in / Sign up

Export Citation Format

Share Document