Gluconeogenesis in biotin deficiency: In vivo synthesis of pyruvate holocarboxylase in biotin deficient rat liver

Deodhar, A.D.; Mistry, S. P.

doi:10.1016/0006-291x(69)90243-5

Cited by 38 publications

(11 citation statements)

References 12 publications

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“…1978; Walton, Cowey & Adron 1984) and mammals (Arinze & Mistry 1971). It is generally recognized that the activities of biotin enzymes are reduced in biotin‐deficient animals (Deodhar & Mistry 1969; Arinze & Mistry 1971). In the present study, both pyruvate carboxylase and acetyl CoA carboxylase activities in the liver were significantly lower in fish fed the control diet than in fish fed the biotin‐supplemented diets.…”

Section: Discussionmentioning

confidence: 99%

Dietary biotin requirement determined for Indian catfish, Heteropneustes fossilis (Bloch), fingerlings

Mohamed¹

2001

Aquaculture Research

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Triplicate groups of Indian catfish, Heteropneustes fossilis (Bloch), fingerlings (average wet weight 3.55 ± 0.03 g) were fed semi‐purified diets containing six levels of biotin (0, 0.086, 0.26, 0.86, 2.5 and 4.3 mg kg−1 diet) for 15 weeks. After 42 days of feeding, fish fed the control (no biotin) diet had developed severe deficiency signs characterized by convulsions, heavy mortality, listlessness, poor feed conversion and feed intake, dark skin colour, tetanus and weight loss. None of these signs was seen in fish fed biotin‐supplemented diets. Among all the biotin‐supplemented diets, percentage weight gain was significantly highest for fish fed the diet supplemented with 0.26 mg of biotin kg−1 and significantly lowest for fish fed the diet supplemented with 0.086 mg of biotin kg−1. Feed conversion ratio (FCR) and protein efficiency ratio (PER) patterns were similar to that of percentage weight gain. The carcass protein and lipid contents were influenced by the dietary biotin up to fish fed 0.26 mg of biotin kg−1. Significantly higher body biotin content, liver pyruvate carboxylase and acetyl CoA carboxylase activities were observed in fish fed biotin‐supplemented diets than in fish fed the control diet. Broken‐line analyses showed that the optimum dietary requirement for biotin for maximal weight gain, body biotin content, liver pyruvate carboxylase and acetyl CoA carboxylase activities was about 0.25 mg kg−1. Associated liver pyruvate carboxylase and acetyl CoA carboxylase activities for normal growth ranged from 105 to 120 units mg−1 protein and from 9 to 11 units mg−1 protein respectively.

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Section: Discussionmentioning

confidence: 99%

Dietary biotin requirement determined for Indian catfish, Heteropneustes fossilis (Bloch), fingerlings

Mohamed¹

2001

Aquaculture Research

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“…All enzyme preparations were done at 0-4O. Samples for pyruvate carboxylase and propionyl CoA carboxylase were prepared by homogenizing the liver and sonicating the homogenate ( 5 % ) in a 0.25 M sucrose medium containing 0.02 M Tris-HC1 buffer, pH 7.4, 1 mM reduced glutathione (GSH) and 1 mM EDTA (11). Livers from eight embryos were pooled and homogenized in 5-10 ml of medium.…”

mentioning

confidence: 99%

“…1). After hatching, the enzyme activity progressively declined to minimal values in [10][11][12][13][14] days, only to display a pronounced increase in the third week. Thereafter, the activity profile showed no further significant changes until adulthood.…”

mentioning

confidence: 99%

Hepatic Acetyl CoA Carboxylase, Propionyl CoA Carboxylase and Pyruvate Carboxylase Activities During Embryonic Development and Growth in Chickens

Arinze¹,

Mistry²

1970

Experimental Biology and Medicine

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“…Chickens were killed by cervical dislocation, and liver, kidney, heart, and brain were removed quickly and dropped into ice-cold homogenizing medium (Deodhar and Mistry, 1969). Samples for enzyme assays were prepared in the cold room (0-4 C.) by homogenizing the tissues (10 percent W./V.)…”

Section: Animalsmentioning

confidence: 99%

“…Pyruvate carboxylase was assayed as described by Deodhar and Mistry (1969). Propionyl CoA carboxylase was measured essentially according to the method of Lane and Halenz (1962).…”

Section: Animalsmentioning

confidence: 99%

Activities of Pyruvate and Propionyl Coenzyme A Carboxylase in Chicken Tissues During Normal Growth and Biotin Deficiency

Shen

Mistry

1977

Poultry Science

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Activities of pyruvate and propionyl CoA carboxylase in chicken tissues during normal growth and biotin deficiency were investigated. In normal growing chickens, liver and kidney pyruvate carboxylase activity was high and varied with age. The activity in heart and brain was low and remained relatively constant throughout the experimental period. Propionyl CoA carboxylase activity in kidney and heart appeared to increase with age but remained unchanged in liver and brain. Biotin deficiency progressively decreased both pyruvate and propionyl CoA carboxylase activities in liver, kidney, heart and brain. Most marked effects were observed in liver and kidney.

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Gluconeogenesis in biotin deficiency: In vivo synthesis of pyruvate holocarboxylase in biotin deficient rat liver

Cited by 38 publications

References 12 publications

Dietary biotin requirement determined for Indian catfish, Heteropneustes fossilis (Bloch), fingerlings

Dietary biotin requirement determined for Indian catfish, Heteropneustes fossilis (Bloch), fingerlings

Hepatic Acetyl CoA Carboxylase, Propionyl CoA Carboxylase and Pyruvate Carboxylase Activities During Embryonic Development and Growth in Chickens

Activities of Pyruvate and Propionyl Coenzyme A Carboxylase in Chicken Tissues During Normal Growth and Biotin Deficiency

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