Results 211 to 220 of about 218,823 (239)

Prolidase‐proline dehydrogenase/proline oxidase‐collagen biosynthesis axis as a potential interface of apoptosis/autophagy

BioFactors, 2016
AbstractProlidase is a cytosolic imidodipeptidase that specifically splits imidodipeptides with C‐terminal proline or hydroxyproline. The enzyme plays an important role in the recycling of proline from imidodipeptides for resynthesis of collagen and other proline‐containing proteins.
Ilona Oscilowska, Jerzy Palka
exaly   +3 more sources

Proline oxidase in cultured mammalian cells

Journal of Cellular Physiology, 1977
AbstractWe sought a cultured cell line with Proline Oxidase activity to study the regulation and physiologic role of the enzyme in mammalian tissues. Among the cell lines tested, only LLC‐RK1 cells, derived from rabbit kidney, had significant Proline Oxidase activity; the Km for proline of the enzyme from these cells was similar to that for the liver ...
S J, Downing, J M, Phang, E M, Kowaloff, D, Valle, R J, Smith   +4 more
openaire   +2 more sources

PROLINE OXIDASES IN HANSENULA SUBPELLICULOSA

Journal of Bacteriology, 1964
Ling, Chung-Mei (Illinois Institute of Technology, Chicago), and L. R. Hedrick . Proline oxidases in Hansenula subpelliculosa . J. Bacteriol. 87: 1462–1470.
C M, LING, L R, HEDRICK
openaire   +2 more sources

Glucocorticoid control of hepatic proline oxidase

Metabolism, 1977
Since adrenal corticosteroids are known to affect amino acid metabolism and gluconeogenesis, we examined the relationship of these hormones to hepatic proline oxidase, the mitochondrial enzyme degrading L-proline. In adrenalectomized rats hepatic proline oxidase activity decreased to about 50% of control levels within 5-6 days.
E M, Kowaloff, A S, Granger, J M, Phang
openaire   +2 more sources

Characteristics of proline oxidase in rat tissues.

Journal of biochemistry, 1980
In adult rats the activity of proline oxidase is high in the liver and kidney and moderate in the brain and heart, but it is not detectable in the lung, skeletal muscle, spleen, or small intestine. The activity in the liver is 1.5 times higher in females than males.
Y, Kawabata, N, Katunuma, Y, Sanada
openaire   +3 more sources

Proline oxidase inhibition by free fatty acids of rat pancreas

Biochimica Et Biophysica Acta - Biomembranes, 1980
Proline oxidase activity was not measurable in pancreas homogenate but was measurable in pancreas slices. Moreover, added pancreas homogenate inhibited proline oxidase activity in rat liver mitochondria and several other tissues. The partially purified inhibitor from pancreas also inhibited the activity of glutamate, glucose 6-phosphate, NADH and ...
W Eugene Knox, W E Knox
exaly   +3 more sources

Proline accumulation by mutation or disruption of the proline oxidase gene improves resistance to freezing and desiccation stresses inSaccharomyces cerevisiae [PDF]

FEMS Microbiology Letters, 2000
Hiroshi Takagi, Shigeru Nakamori
exaly   +2 more sources

Glucocorticoid induction of proline oxidase in LLC‐RK1 cells

Journal of Cellular Physiology, 1978
AbstractDexamethasone induced proline oxidase in cultured LLC‐RK1 cells, an epithelial cell line derived from rabbit kidney. The dexamethasone‐mediated increase in enzyme activity was concentration and time dependent. Although the effect could be dissociated from cell growth and cell density, it was dependent on protein and RNA synthesis.
E M, Kowaloff, J M, Phang, A S, Granger, S J, Downing   +3 more
openaire   +2 more sources

Expression in Escherichia coli of the catalytic domain of human proline oxidase

Protein Expression and Purification, 2012
The human PRODH gene has been shown to have unique roles in regulating cell survival and apoptotic pathways and it has been related to velocardiofacial syndrome/DiGeorge syndrome and increased susceptibility to schizophrenia. It encodes for the flavoprotein proline oxidase (PO), which catalyzes the conversion of l-proline to Δ(1)-pyrroline-5 ...
Loredano Pollegioni, Gianluca Molla, Stefano Servi   +2 more
exaly   +4 more sources

d-Amino acid oxidase and presence of d-proline in Xenopus laevis

Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology, 2013
We purified D-amino acid oxidase (EC 1.4.3.3, DAO) from Xenopus laevis tadpoles. The optimal temperature and pH for enzyme activity were 35-40 °C and 8.3-9.0, respectively, depending on the substrate amino acids available to the enzyme; the highest activity was observed with D-proline followed by D-phenylalanine. Activity was significantly inhibited by
Yoko Nagata, Minoru Tanigawa
exaly   +3 more sources