doi: 10.1073/pnas.76.12.6323.
Changes in activity of fructose-1,6-bisphosphate aldolase in livers of fasted rabbits and accumulation of crossreacting immune material
- PMID: 293723
- PMCID: PMC411856
- DOI: 10.1073/pnas.76.12.6323
Item in Clipboard
Changes in activity of fructose-1,6-bisphosphate aldolase in livers of fasted rabbits and accumulation of crossreacting immune material
Proc Natl Acad Sci U S A.
1979 Dec.
Abstract
The activity of fructose-1,6-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) in livers of fasted rabbits decreases to less than one-half the value found in livers of fed rabbits. However, the concentration of aldolase protein in the liver extracts, measured with a specific antibody, remains unchanged. More than twice as much antibody is required to neutralize the aldolase activity in liver extracts from fasted compared with fed rabbits. The results suggest that modification of liver aldolase occurs during fasting, resulting in loss of catalytic activity without loss of immunoreactivity.
Similar articles
-
Characterization of the inactive form of fructose-1,6-bisphosphate aldolase isolated from livers of fasted rabbits.Proc Natl Acad Sci U S A. 1982 Sep;79(17):5194-6. doi: 10.1073/pnas.79.17.5194. Proc Natl Acad Sci U S A. 1982. PMID: 6957858 Free PMC article.
-
Proteolytic modification of rat liver fructose-1,6-bisphosphate aldolase by administration of leupeptin in vivo.Biochim Biophys Acta. 1981 Jun 15;659(2):378-89. doi: 10.1016/0005-2744(81)90064-4. Biochim Biophys Acta. 1981. PMID: 7020765
-
Inactivation of liver aldolase in fasting rabbits: evidence for the accumulation of two different immunoreactive forms.Arch Biochem Biophys. 1980 Aug;203(1):390-4. doi: 10.1016/0003-9861(80)90191-5. Arch Biochem Biophys. 1980. PMID: 7406507 No abstract available.
-
Kinetic and immunological abnormalities of aldolase B in herediatry fructose intolerance.Biochem Soc Trans. 1975;3(2):232-4. doi: 10.1042/bst0030232. Biochem Soc Trans. 1975. PMID: 805723 Review. No abstract available.
-
Fructose 1,6-bisphosphate aldolase: A promising prognostic marker for oral cancer and its role in radiotherapy response.Radiother Oncol. 2024 Nov;200:110537. doi: 10.1016/j.radonc.2024.110537. Epub 2024 Sep 13. Radiother Oncol. 2024. PMID: 39278318 Review.
Cited by
-
Limited proteolysis of liver aldolase and fructose 1,6-bisphosphatase by lysosomal proteinases: effect on complex formation.Proc Natl Acad Sci U S A. 1982 Apr;79(8):2451-4. doi: 10.1073/pnas.79.8.2451. Proc Natl Acad Sci U S A. 1982. PMID: 6283526 Free PMC article.
-
Characterization of the inactive form of fructose-1,6-bisphosphate aldolase isolated from livers of fasted rabbits.Proc Natl Acad Sci U S A. 1982 Sep;79(17):5194-6. doi: 10.1073/pnas.79.17.5194. Proc Natl Acad Sci U S A. 1982. PMID: 6957858 Free PMC article.
-
Identification of intracellular degradation intermediates of aldolase B by antiserum to the denatured enzyme.Proc Natl Acad Sci U S A. 1985 Sep;82(18):6114-8. doi: 10.1073/pnas.82.18.6114. Proc Natl Acad Sci U S A. 1985. PMID: 3898080 Free PMC article.
-
Shikonin, vitamin K3 and vitamin K5 inhibit multiple glycolytic enzymes in MCF-7 cells.Oncol Lett. 2018 May;15(5):7423-7432. doi: 10.3892/ol.2018.8251. Epub 2018 Mar 13. Oncol Lett. 2018. PMID: 29725454 Free PMC article.
References
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
