The electrophoretic distribution and substrate specificities of isozymes of glucose-6-phosphate dehydrogenase (E.C. 1.1.1.49) were studied in seven species of teleost fish. The fish examined included two species of bonefish, Albula neoguinaica and A. glossodonta (Albulidae, Anquilliformes) (Shaklee
Comparative study on glucose-6-phosphate dehydrogenase from rabbit tissues
β Scribed by Ninfali, Paolino ;Palma, Fulvio
- Publisher
- John Wiley and Sons
- Year
- 1990
- Tongue
- English
- Weight
- 666 KB
- Volume
- 254
- Category
- Article
- ISSN
- 0022-104X
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β¦ Synopsis
Abstract
The activity of glucoseβ6βphosphate dehydrogenase (G6PD) was measured in bone marrow, spleen, lung, liver, kidney, adipose tissue, brain, heart, muscle, and in the erythroid cell line of rabbit. In tissues, the activity ranged from 6.87 to 0.09 U/g wet tissue, found in bone marrow and muscles, respectively, whereas in the erythroid cell line it ranged from 14.3 to 2.4 U/g cells for erythroblasts and erythrocytes, respectively. The electrophoretic patterns of the tissue crude extracts shoed an identical set of three activity bands, and the immunotitration curves obtained with rat antirabbit erythrocyte G6PD antibodies shared the same equivalence point. The enzyme, purified to homogeneity from different tissues, showed no significant differences among the Km values for NADP and G6P. The results give a picture of the variability of the G6PD activity in rabbit tissues and suggest the presence of the same enzyme molecule in each tissue.
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