catabolize


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Synonyms for catabolize

subject to catabolism

References in periodicals archive ?
These enzymes when confronted with some abnormal light chains cannot adequately catabolize them owing to their peculiar physicochemical characteristics.
An important function of the kidneys is to re-absorb and catabolize small proteins, such as free light chains.
The bacterium's ability to catabolize biphenyls is directly related to the presence of a locus of approximately thirteen genes known as the bph cluster.
One role of kidney function is to catabolize certain plasma proteins and polypeptides.
During pro-longed recoveries, patients can catabolize up to one-tenth of their muscle mass despite putting on weight.
Chronic, excessive intake of protein (or any macronutrient) elevates the activity of enzymes that catabolize it or convert it to fat.
The metabolite, or waste product, of serotonin is produced by the enzymes monoamine oxidase (MAO) and aldehyde oxidase, which together catabolize serotonin to the waste metabolite 5-hydroxy indole acetic acid (5-HIAA), which is excreted via the cerebrospinal fluid (CSF) and the blood.
A second bioassay, the biodegradable organic carbon (BDOC) assay, is based on the activity of the indigenous microflora, particularly the ability to catabolize organic carbon to carbon dioxide.
glutathione, vitamins E and C, and [beta]-carotene [33], lipoic acid, ubiquinone, and urate) and enzymatic systems that catabolize ROS physiologically generated [25].
Most recently, an archaea strain known as Methanomassiliicoccus luminyensis B10 was found to be able to catabolize TMA.
3]-N concentration between T1 and T2 suggests that proteolytic microbes may catabolize the proteinaceous substances in the MRS medium added to these treatment groups.
This distinction is fundamental in cephalopods, because they digest lipids poorly and their capacity to catabolize them is limited (Navarro & Villanueva 2000, Garcia Garcia & Aguado Gimenez 2002).
light chains escape glomerular charge and size barriers and overwhelm tubular capacity to reabsorb and catabolize them.
Both in laboratory and field situations, low concentrations of DOM may force larvae to catabolize endogenous reserves to fuel development, while larvae in DOM-rich seawater may be able to utilize those exogenous sources of energy, thereby sparing endogenous reserves (Jaeckle and Manahan, 1992).
1] The disorder is caused by an enzyme deficiency that results in an inability to catabolize homogentisic acid, an intermediary component in the metabolism of tyrosine and phenylalanine.