A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol
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منابع مشابه
DNase I-like endonuclease in rat kidney cortex that is activated during ischemia/reperfusion injury.
Ischemia/reperfusion is known to result in DNA fragmentation and cell death in kidney tubular epithelium, but the endonucleases responsible for this DNA damage have not been identified. DNA substrate gel analysis of extracts from normal rat kidney cortex revealed the presence of a DNase with an apparent molecular mass of 30 to 34 kD. This enzyme is not a dimer of the previously described nuclea...
متن کاملNephron Segments of Rat Kidney Cortex
Renal cortical tubules consist of polarized epithelial cells where Na/H antiport activity has been demonstrated on the apical and/or basolateral membrane. Apical Na/H antiport activity plays an important role in transcellular bicarbonate (HCO3) reabsorption, whereas basolateral Na/H antiport activity could be involved in transcellular HCO3secretion as well as cell volume and pH control. To dete...
متن کاملA New Phosphodiesterase in Rat Tissues
1. A phosphodiesterase that cleaves glycerophosphoinositol into glycerophosphate and inositol has been detected in rat tissues. 2. The enzyme requires Mg2+(Mn2+) and has a pH optimum of 7.7. 3. The richest sources of the enzyme are kidney and intestinal mucosa. In pancreas subcellular fractions it occurs largely in the microsomal fraction. 4. The enzyme is inhibited by excess substrate and by t...
متن کاملRenin substrate in granules from rat kidney cortex.
1. Subcellular fractions of rat kidney cortex generated angiotensin I continuously over 2h when incubated at 37degreesC with rat renin, indicating the presence of renin substrate within cells in the renal cortex. 2. Renin substrate was located in highest specific concentration in particulate fractions. The particles containing renin substrate had a sedimentation velocity slightly lower than mit...
متن کاملThe subcellular localization of glutaminase isoenzymes in rat kidney cortex.
The subcellular localization of the isoenzymes of glutaminase has been studied in rat renal cortex. Differential and sucrose density centrifugation techniques demonstrated a mitochondrial localization for phosphate-dependent glutaminase. Fractionation of isolated mitochondria by digitonin and by sonication revealed a matrix localization for phosphate-dependent glutaminase, a finding in agreemen...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1977
ISSN: 0306-3283
DOI: 10.1042/bj1620241