Early conformational changes and activity modulation induced by guanidinium chloride on intestinal alkaline phosphatase
نویسندگان
چکیده
منابع مشابه
Chicken Intestinal Alkaline Phosphatase
Purified chicken intestinal alkaline phosphatase is active at pH 8 to 9, but becomes rapidly inactivated with change of pH to 6 or less. Also, a solution of the inactivated enzyme at pH 4.5 rapidly regains its activity at pH 8. In the range of pH 6 to 8 a solution of purified alkaline phosphatase consists of a mixture of active and inactive enzyme in equilibrium with each other. The rate of ina...
متن کاملHuman Intestinal Alkaline Phosphatase
HUMAN INTESTINAL ALKALINE PHOSPHATASE. Tissue expression and serum levels. ISBN 91-7174-674-9 ISSN 0346-6612 New series No 342 Ulla Domar, Department of Medical Biochemistry and Biophysics, University of Umeå, S-90187 Umeå, Sweden. Human alkaline phosphatase (ALP) comprises four isozymes, viz liver/bone/ kidney or tissue unspecific (AP), intestinal (LAP), placental (PLAP) and germ cell or PLAP-...
متن کاملEarly weaning reduces small intestinal alkaline phosphatase expression in pigs.
Expression of the small intestinal alkaline phosphatase (IAP) is enterocyte differentiation dependent and plays essential roles in the detoxification of pathogenic bacterial lipopolysaccharide endotoxin, maintenance of luminal pH, organic phosphate digestion, and fat absorption. This study was conducted to examine the effect of early weaning on adaptive changes in IAP digestive capacity (V(cap)...
متن کاملCholesterol modulates alkaline phosphatase activity of rat intestinal microvillus membranes.
Experiments were conducted, using a nonspecific lipid transfer protein, to vary the cholesterol/phospholipid molar ratio of rat proximal small intestinal microvillus membranes in order to assess the possible role of cholesterol in modulating enzymatic activities of this plasma membrane. Cholesterol/phospholipid molar ratios from 0.71 to 1.30 were produced from a normal value of 1.05 by incubati...
متن کاملConformational changes at the active site of creatine kinase at low concentrations of guanidinium chloride.
It has been previously reported that, during denaturation of creatine kinase by guanidinium chloride (GdmCl) or urea [Tsou (1986), Trends Biochem. Sci. 11, 427-429], inactivation occurs before noticeable conformational change can be detected, and it is suggested that the conformation at the active site is more easily perturbed and hence more flexible than the molecule as a whole. In this study,...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1987
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2480551