Serum glucuronidase activity

Kikuchi, H., Y. Suzuki, and Y. Hashimoto. 1981. Increase of (3-glucuronidase activity in the serum of rats administered organophosphate and carbamate insecticides. Jour. Toxicol. Sci. 6 27-35. 

Serum (3-glucuronidase activity was increased in a dose-related manner when disulfoton was given intraperitoneally to rats (Kikuchi et al. 1981). In the same study, this effect was not observed in mice, rabbits, or guinea pigs. This enzyme appears to be a useful biomarker of hepatic function in rats exposed to disulfoton, but may not be a useful biomarker in humans. 

The (3-glucuronidase activity of human blood has been studied by Fishman and co-workers.26 The range in 230 normals was found to be from 41 to 1285 units per 100 ml. of serum. In the diseased subjects studied, the minimum values tended to be higher and the maximum values were up to 2340 units. 

Lampe, J.W., Li, S.S., Potter, J.D., and King, I.B., Serum p-glucuronidase activity is inversely associated with plant-food intakes in humans, J. Nutr., 132, 1341, 2002. 

In cases of low -glucuronidase activity, the activity of this enzyme in serum should also be assessed to avoid missing I - cell disease. 

There was no significant difference between the serum j8-glucuronidase activities before and after the bypass. However, the serum acid phosphatase was higher, in each of the patients but one, after the bypass than before, and the mean value was significantly higher. The basis for the increased serum activity of one lysosomal enzyme, acid phosphatase, but not that of another, /3-glucuronidase, is of interest. It is possible, as Chiu et al. (C2) have suggested, that the increased acid phosphatase... 

Injection of alkyl phosphates into rats raised the level of P-D-glucuronidase activity in their sera without affecting the levels of lysosomal hydrolases and cholinesterase. Dibutyl and tributyl phosphates were most and equally effective, the levels of P-D-glucuronidase activity increasing 120- and 90-fold after 1 and 2 h, respectively. The increase in enzymic activity elicited with tributyl phosphate correlated with a lowering of the enzymic activity in the liver microsomes, which appear to be the main source of the excess of P-D-glucuronidase activity in the serum. 

A study of the glycoside hydrolases of human lung showed that the level of -D-glucuronidase activity is low. The electrophoretic mobility of the enzyme on polyacrylamide gels indicated that it is different from serum jS-o-glucuroni-dase. The secretory mechanism of the lung enzyme was discussed. ... 

Following treatment of intact rats with cortisone for 1-2 weeks, the /3-glucuronidase activity w as enhanced distinctly, not only in adrenals and testes but also in the liver, kidney, thymus, seminal vesicle, and serum (Murakami, 1961a). Adrenalectomy produced little effect on rat tissues. 

J here were no significant differences in the serum level of d-glucuronidase between virgin rats without arterial disease and breeder rats with atherosclerosis. J emale breeders with athenxsclerosis showed an increase of jS-glucuronidase activity in the aortic arch and abdominal sections (Wexler and Judd, 1966). 

Serum and urinary S-glucuronidase activity is normal in lung cancer patients. The activities of 9-g ucuronidaae and other enzymes has been shown by biochemical and liistoeliemical methods to be consistently higher in lung cancer tissue than in normal lung tissue (Suzuki, 1966 Kanayama,... 

Also, before one can choose the substrate concentration for a particular method, the Michaelis constant must be determined. Usually, if the enzyme does not exhibit inhibition at high substrate concentration, it may be reasonable to use a working molar concentration of the substrate equal to 3 or 4 times the Km value so that the enzyme can manifest its highest activity. As in the case of j8-glucuronidase (F17), the conditions developed for a particular isoenzyme (of alkaline phosphatase) in one tissue may not be applicable for another isoenzyme in another tissue or for those present in serum. Hence reevaluation of every reaction condition (e.g., substrate concentration, optimum pH) is necessary for each isoenzyme. Vide infra 2.1.1. 

A dodecasaccharide that was obtained by hydrolysis of dermatan sulphate with testicular hyaluronidase, chondroitin lyase AC, and jS-D-glucuronidase yielded a sulphated 2-amino-2-deoxy-D-galactose derivative when treated with human serum at pH 4.5 or 7.0. No further degradation of the substrate occurred, suggesting that normal human serum possesses an cxo-jS-D-acetamidodeoxyhexosidase that is active towards dermatan sulphate. 

Homogenates from irradiated mouse mammary tumor showed an increase of total activities of lysosomal enzymes and a shift from sediment le toward unsedimentable activity. These biochemical changes were accompanied by an increase in the value of /S-glucuronidase level in both serum and urine (Watts et d., 1966),... 

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