Changes in kinetic properties of pyridoxal-dependent enzymes during dietary vitamin B6 deficiency in rats
The erythrocyte aspartate aminotransferase and renal and intestinal glycogen phosphorylase activities in rats are determined as dependent on their provision with vitamin B6. It has been shown that the aspartate aminotransferase activity decreases and the shape of the aspartate concentration-activity...
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Published in: | Ukrainskij biohimičeskij žurnal Vol. 62; no. 1; p. 44 |
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Format: | Journal Article |
Language: | Russian |
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Ukraine
01-01-1990
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Abstract | The erythrocyte aspartate aminotransferase and renal and intestinal glycogen phosphorylase activities in rats are determined as dependent on their provision with vitamin B6. It has been shown that the aspartate aminotransferase activity decreases and the shape of the aspartate concentration-activity curve changes in the vitamin B6-deficient animals. The B6 insufficiency does not affect the intestinal mucosa glycogen phosphorylase. However the renal phosphorylase activity decreases by 30 percent in the vitamin B6 deficient rats. It occurs due to changes in the affinity of phosphorylase A and B to glucose-1-phosphate but not to AMP. The activation of these investigated enzymes by exogenous pyridoxal phosphate reveals no essential differences between the vitamin B6-deficient and normal rats. The possible causes of the observed changes in the aspartate aminotransferase and phosphorylase activity are discussed. |
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AbstractList | The erythrocyte aspartate aminotransferase and renal and intestinal glycogen phosphorylase activities in rats are determined as dependent on their provision with vitamin B6. It has been shown that the aspartate aminotransferase activity decreases and the shape of the aspartate concentration-activity curve changes in the vitamin B6-deficient animals. The B6 insufficiency does not affect the intestinal mucosa glycogen phosphorylase. However the renal phosphorylase activity decreases by 30 percent in the vitamin B6 deficient rats. It occurs due to changes in the affinity of phosphorylase A and B to glucose-1-phosphate but not to AMP. The activation of these investigated enzymes by exogenous pyridoxal phosphate reveals no essential differences between the vitamin B6-deficient and normal rats. The possible causes of the observed changes in the aspartate aminotransferase and phosphorylase activity are discussed. |
Author | Kodentsova, V M Glinka, E Iu |
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BackLink | https://www.ncbi.nlm.nih.gov/pubmed/2110692$$D View this record in MEDLINE/PubMed |
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DocumentTitleAlternate | Izmenenie kineticheskikh svoĭstv piridoksal'zavisimykh fermentov pri alimentarnoĭ nedostatochnosti vitamina B6 u krys |
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SubjectTerms | Animals Aspartate Aminotransferases - blood Aspartate Aminotransferases - deficiency Diet Erythrocytes - enzymology Humans Kidney - enzymology Kinetics Male Phosphorylase a - blood Phosphorylase a - deficiency Phosphorylase b - blood Phosphorylase b - deficiency Phosphorylases - deficiency Rats Rats, Inbred Strains Species Specificity Vitamin B 6 Deficiency - enzymology |
Title | Changes in kinetic properties of pyridoxal-dependent enzymes during dietary vitamin B6 deficiency in rats |
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