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Histoenzymological localization of glycerol 3 phosphate dehydrogenase and succinate dehydrogenase in the mesencephalon of a minor carp Barilius bendelisis (Hamilton)

100%

Singh N.

Acta Ichthyologica et Piscatoria

1988

tom 18

nr 2

Mitochondria as oxidative signalling organelles in T-cell activation: physiological role and pathological implications

84%

Kaminski M. M. , Roth D. , Krammer P. H. , Gulow K.

tom 61

nr 5

Long-chain orcinol homologs from cereal bran are effective inhibitors of glycerophosphate dehydrogenase

67%

Rejman J. , Kozubek A.

Cellular and Molecular Biology Letters

1997

tom 02

nr 4

It was found that 5-n-alk(en)ylresorcinols isolated from high-fiber diet, wheat or rye bran, effectively inhibit glycerol-3-phosphate dehydrogenase (GPDH, EC 1.1.1.8), the key enzyme of triacylglycerol synthesis in adipocytes. The concentration of alk(en)ylresorcinols necessary for 50 per cent inhibition of GPDH vary from 3.8 µM to 6.4 µM. The effectiveness of the inhibition depends on the length of alk(en)enylresorcinol side chain and hydrophilic ring substitutions. The effectivity of homologs with long side chain (C17 and C19) in apparent inhibition of GPDH is slightly higher than that reported previously for adipostatin A (5-n-pentadecylresorcinol) isolated from Streptomyces (Tsuge, N., Mizokami, M., Imai, S., Shimazu, A., & Seto, H. (1992) J. Antibiot. 45, 886- 891). The fact that the studied resorcinols are natural components of high-fiber human diet, such as porridge and bran products, suggests their possible participation in prevention of the risk of corpulence.