Disaccharidase of rabbit small intestine: Intracellular distribution, solubilization, purification and specificity

Gitzelmann, R; Davidson, Eugene A.; Osinchak, Joseph

doi:10.1016/0926-6569(64)90168-3

Cited by 6 publications

(3 citation statements)

References 21 publications

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“…Soluble intestinal maltase activity has been found to represent a very small fraction of total intestinal maltase activity whenever measured previously, ranging from 1.2 to 11.0% in a variety of species, including rabbit (Gitzelmann et al, 1963), chicken (Siddons, 1970), human (Auricchio et al, 1963) and monkey (Swaminathan & Radhakrishnan, 1970). Foetal or neonatal mammals have not been studied, however, so that this experience must be regarded only as typical of the weaned animal.…”

Section: Discussionmentioning

confidence: 74%

Soluble neutral and acid maltases in the suckling-rat intestine. The effect of cortisol and development

Galand

Forstner

1974

Biochemical Journal

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The 100000g supernatants from 13-day-old suckling-rat intestinal homogenates contained 43.5% of the total intestinal maltase activity, compared with 7.1% in weaned adult rats aged 40 days. The soluble maltase activity was separated on Sepharose 4B into two quantitatively equal fractions at pH6.0, one containing a maltase with a neutral pH optimum and the other a maltase with an acid pH optimum. The neutral maltase was shown to be a maltase-glucoamylase identical with membrane-bound maltase-glucoamylase in molecular weight, heat-sensitivity, substrate specificity, K(m) for maltose and K(i) for Tris. The soluble enzyme was induced by cortisol, but the ratio of the soluble to bound enzyme fell during induction. Solubility of the neutral maltase was not accounted for by the action of endogenous proteinases under the preparative conditions used. It is postulated that the soluble neutral maltase is a membrane-dissociated form of the bound enzyme and that the relationship between these two forms is modulated by cortisol. The acid maltase generally resembled acid maltase of liver, muscle and kidney. It was shown to be a maltase-glucoamylase with optimal activity at pH3.0, and molecular weight of 136000 by density-gradient centrifugation. At pH3.0 its K(m) for maltose was 1.5mm. It was inhibited by turanose (K(i)=7.5mm) and Tris (K(i)=5.5mm) but not by p-chloromercuribenzoate or EDTA. Some 55% of its activity was destroyed by heating at 50 degrees C for 10min. The acid maltase closely resembled beta-glucuronidase and acid beta-galactosidase in its distribution in the intestine, response to tissue homogenization in various media, and decrease in activity with cortisol treatment and weaning, indicating that it was a typical lysosomal enzyme concentrated in the ileum.

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Section: Discussionmentioning

confidence: 74%

Soluble neutral and acid maltases in the suckling-rat intestine. The effect of cortisol and development

Galand

Forstner

1974

Biochemical Journal

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“…Although P-galactosidase is one of the enzymes associated with lysosomal particles in the liver, in other organs different cell fractions may be major sites of activity, as already noted for intestine, and in this case the apparent distribution depended on the substrate used. Other disaccharidases in small intestine have also been shown to have a different distribution from that of acid phosphatase (Gitzelmann, Davidson & Osinchak, 1964). There have been several other indications in the literature that the commonly used nitrophenyl substrates do not always present a complete or typical picture of enzyme activity.…”

Section: Discussionmentioning

confidence: 99%

Specificity and multiple forms of β-galactosidase in the rat

Furth

Robinson

1965

Biochemical Journal

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1. Ten rat tissues and organs have been assayed for beta-galactosidase with phenyl beta-d-galactoside, p-nitrophenyl beta-d-galactoside, p-aminophenyl beta-d-galactoside and 4-methylumbelliferyl beta-d-galactoside as substrates. 2. The relative activities of these tissues are independent of the mode of assay, and maximum rates of hydrolysis are not greatly affected by the nature of the substrate. 3. Inhibition studies suggest the liver enzyme has no associated beta-glucosidase activity. 4. There is no cellular localization of preferential activity towards any of the four substrates in liver, kidney or spleen. 5. Evidence suggesting the non-destructive penetration of liver lysosomal membranes by p-nitrophenyl beta-d-galactoside is presented. 6. Liver lysosomal beta-galactosidase exists in multiple forms that can be separated on DEAE-cellulose, and the enzyme components that are bound to the membrane appear to be similar to those of the lysosome sap. 7. The chromatographic pattern of enzyme excreted in the urine is compared with those from the kidney, intestine, spleen and liver.

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“…Moreover, it is recognized that the lining cells of the villi explain an important function regarding the absorption of sugars, because they contain disaccharidase activities localized in the brush border [4,6,9].…”

Section: It Is Also Known That the Intestinal Wall Of Mice Infected mentioning

confidence: 99%

Disaccharidase Content in the Small-intestinal Mucosa of Normal Mouse and of Mouse with Viral MHV-3 Hepatitis

Filosa¹,

Balestrieri²,

Ruggiero³

et al. 1970

Enzymol Biol Clin

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The authors studied the disaccharidase activities (lactase, palatinase, sucrase, maltase) in the intestinal mucosa of normal and MHV-3 virus infected mice. No significant differences were observed upon statistical analysis between the enzymatic activities of normal and MHV-3 infected mice. The authors have studied also the coefficients of correlation 'r', between the various disaccharidase activities in normal animals. This coefficient 'r' is an extremely valuable statistical tool for detecting associations between continuous variables. By this statistical analysis it appears that the correlation existing between the various disaccharidase activities are all statistically significant. Moreover the authors have calculated the coefficiente of linear regression 'b'. The calculated values of the coefficients 'b', between the various enzymatic activities, consent, by the determination of only one disaccharidase activity, to forecast statistically the values of the others.

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Disaccharidase of rabbit small intestine: Intracellular distribution, solubilization, purification and specificity

Cited by 6 publications

References 21 publications

Soluble neutral and acid maltases in the suckling-rat intestine. The effect of cortisol and development

Soluble neutral and acid maltases in the suckling-rat intestine. The effect of cortisol and development

Specificity and multiple forms of β-galactosidase in the rat

Disaccharidase Content in the Small-intestinal Mucosa of Normal Mouse and of Mouse with Viral MHV-3 Hepatitis

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