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Literature DB >> 113252

The localization of mutarotase in rat kidney.

S Baba, Y Arimoto, D Yoshikawa, Y Toyoda, I Miwa, J Okuda.

Abstract

The localization of mutarotase in rat kidney was investigated by fluorescein-labelled and peroxidase-labelled antibody techniques, and by method of isolation of the nuclei and cytoplasm in non-aqueous solvents. In these immunohistochemical studies, mutarotase was almost exclusively recognized in the nuclei of epithelial cells of renal tubules and glomeruli in rat. The specific activity of mutarotase was found to be 1.5 times higher in the nuclei (122 units/g dry wt) than that in the cytoplasm (80 units/g dry wt) isolated with non-aqueous solvents. These results suggest that mutarotase may be involved in the metabolism of D-glucose in nuclei.

Entities: Chemical Species

Mesh：

Substances：
Carbohydrate Epimerases

Year: 1979 PMID： 113252 DOI： 10.1007/bf01949964

Source DB: PubMed Journal: Experientia ISSN： 0014-4754

14 in total

1. A glycoprotein modified with terminal N-acetylglucosamine and localized at the nuclear rim shows sequence similarity to aldose-1-epimerases.

Authors: A Heese-Peck; N V Raikhel
Journal: Plant Cell Date: 1998-04 Impact factor: 11.277

1 in total

The localization of mutarotase in rat kidney.

1. KINETICS AND DISTRIBUTION OF MUTAROTASES AND THEIR RELATION TO SUGAR TRANSPORT.

2. DISTRIBUTION OF A "MUTAROTASE" ACTIVITY IN RAT TISSUES AND POSSIBLE FUNCTION IN ACTIVE TRANSPORT OF SUGARS.

3. Multiple forms of rat kidney mutarotase.

4. A method for the determination of desoxyribonucleic acid, ribonucleic acid, and phosphoproteins in animal tissues.

5. An improved mutarotase assay using beta-D-glucose oxidase and an oxygen electrode.

6. Mutarotase (aldose-1-epimerase) catalyzed anomerization of glucose-6-phosphate.

7. Rapid polarographic mutarotase assay with -D-glucose oxidase.

8. Studies on mutarotases. V. Serum mutarotase levels in renal disease.

9. Multiple forms of human kidney mutarotase.

10. D-Glucose anomeric preference of hexokinases in higher animals.

1. A glycoprotein modified with terminal N-acetylglucosamine and localized at the nuclear rim shows sequence similarity to aldose-1-epimerases.