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An acid hydrolase is an enzyme that works best at acidic pHs.It is commonly located in lysosomes, which are acidic on the inside.Acid hydrolases may be nucleases, proteases, glycosidases, lipases, phosphatases, sulfatases and phospholipases and make up the approximately 50 degradative enzymes of the lysosome that break apart biological matter.
pH is the negative logarithm (or cologarithm) of molar concentration of hydrogen ions in the extracellular fluid. pK a H 2 CO 3 is the cologarithm of the acid dissociation constant of carbonic acid. It is equal to 6.1. [HCO − 3] is the molar concentration of bicarbonate in the blood plasma.
The pH of tears shift throughout a waking day, rising "about 0.013 pH units/hour" until a prolonged closed-eye period causes the pH to fall again. [15] Most healthy individuals have tear pH in the range of 7.0 to 7.7, where bicarbonate buffering is the most significant, but proteins and other buffering components are also present that are ...
3) is present in the plasma fraction; this constitutes the major mechanism for maintaining the pH of blood between 7.35 and 7.45. Outside this narrow range (7.40 ± 0.05 pH unit), acidosis and alkalosis metabolic conditions rapidly develop, ultimately leading to death if the correct buffering capacity is not rapidly restored.
The lumen's pH (~4.5–5.0) [3] is optimal for the enzymes involved in hydrolysis, analogous to the activity of the stomach. Besides degradation of polymers, the lysosome is involved in cell processes of secretion, plasma membrane repair, apoptosis, cell signaling, and energy metabolism. [4] Lysosomes digest material.
3). Physiologically normal intracellular pH is most commonly between 7.0 and 7.4, though there is variability between tissues (e.g., mammalian skeletal muscle tends to have a pH i of 6.8–7.1). [4] [5] There is also pH variation across different organelles, which can span from around 4.5 to 8.0. [6] [7] pH i can be measured in a number of ...
In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]
Glycerol-3-phosphate dehydrogenase (GPDH) is an enzyme that catalyzes the reversible redox conversion of dihydroxyacetone phosphate (a.k.a. glycerone phosphate, outdated) to sn-glycerol 3-phosphate. [2] Glycerol-3-phosphate dehydrogenase serves as a major link between carbohydrate metabolism and lipid metabolism.