Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “ALKALINE PHOSPHATASE”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 955 records · Page 53Linked to original sources

Influence of ascorbic acid on acid and alkaline phosphatase activities in some metabolically active tissues of aspirin treated rats.

ACP and ALP activities in plasma were increased in aspirin treated groups for a period of seven days. Ascorbic acid supplemented groups showed no significant change in plasma ACP activity, but a significant change in ALP activity was found. ACP and ALP activities in liver and kidney were decreased significantly in aspirin treated animals. ACP activities in liver and kidney in ascorbic acid supplemented groups showed no significant changes. No significant alteration of ALP activity in liver was found in ascorbic acid supplemented group but a significant changes was observed in kidney. Supplementation of ascorbic acid in high doses to rats fed aspirin can restore enzyme activities almost to the normal level.

Acid Phosphatase↗

The pho-2A mutant of Neurospora crassa which is deficient in Pi-repressible alkaline phosphatase (EC 3.1.3.1) is also defective in Pi-repressible acid phosphatase (EC 3.1.3.2).

1. The mycelial Pi-repressible acid phosphatase presented p-nitrophenylphosphatase activity with negative cooperativity and Michaelian behavior when synthesized by the wild-type and pho-2A mutant strains of Neurospora crassa, respectively. 2. The major acid phosphatase present in cell extracts of the pho-2A mutant of N. crassa grown in low Pi medium is more thermolabile (t1/2 = 4 min at 54 degrees C, pH 5.4) than that of the wild strain (stable for at least 80 min at 54 degrees C, pH 5.4). 3. The pho-2A mutant of N. crassa secreted a more thermolabile acid phosphatase (t1/2 = 30 min at 50 degrees C, pH 5.4) than the wild strain (t1/2 of at least 80 min at 50 degrees C, pH 5.4). 4. The pho-2A mutant of N. crassa synthesized a more thermolabile acid phosphatase (t1/2 = 37 min at 54 degrees C, pH 5.4) than the wild strain in high Pi medium (t1/2 = 14 min at 54 degrees C, pH 5.4). 5. The pleiotropic nature of the pho-2 locus and its possible involvement in the mechanism of phosphatase secretion by N. crassa are proposed.

4-Nitrophenylphosphatase↗