Intestinal lactase (beta-galactosidase) and other disaccharidase activities of suckling and adult common brushtail possums, Trichosurus vulpecula (Marsupialia:Phalangeridae)

1989 ◽  
Vol 1 (4) ◽  
pp. 315 ◽  
Author(s):  
EA Crisp ◽  
M Messer ◽  
PE Cowan
Keyword(s):  
Brush Border ◽  
The Other ◽  
Trichosurus Vulpecula ◽  
Galactosidase Activity ◽  
Lactase Activity ◽  
Age Related ◽  
Small Intestinal ◽  
Brush Border Enzyme ◽  
Beta Galactosidase ◽  
Age Related Changes

Small-intestinal disaccharidase activities of eight suckling T. vulpecula, aged from 34 to 150 days, and of two adult animals were investigated. Intestinal maltase, isomaltase and sucrase activities increased with age, whereas lactase activities decreased. Trehalase activities were relatively high in all animals and showed no obvious age-related changes. Three separate beta-galactosidase activities, one neutral and two acid, acted on lactose. The neutral beta-galactosidase activity appeared to be due to a brush border enzyme similar to that of eutherian mammals, whereas the acid beta-galactosidases were soluble and probably of lysosomal origin. One of these, acid beta-galactosidase-1, had similar properties to the sole intestinal beta-galactosidase of macropodid marsupials, whereas the other, acid beta-galactosidase-2, has not previously been described. Galactosyl oligosaccharides isolated from macropodid milk were readily hydrolysed by both acid beta-galactosidases but not by the neutral beta-galactosidase. The total intestinal lactase activity in animals aged up to 125 days was due mainly to acid beta-galactosidase-1, whereas in older animals it was due mostly to the neutral beta-galactosidase; this suggests that late in lactation the young T. vulpecula change from a macropodid mode of digestion of galactosyl oligosaccharides to a eutherian mechanism for the digestion of lactose. These findings may have implications for the hand-rearing of orphaned T. vulpecula.

scholarly journals Age related increase of brush border enzyme activities along the small intestine.

Gut ◽  
1988 ◽  
Vol 29 (11) ◽  
pp. 1557-1563 ◽  
Author(s):  
F Raul ◽  
F Gosse ◽  
M Doffoel ◽  
P Darmenton ◽  
J Y Wessely
Keyword(s):  
Small Intestine ◽  
Brush Border ◽  
Enzyme Activities ◽  
Age Related ◽  
Brush Border Enzyme ◽  
Related Increase

scholarly journals Age-related modulation of plasmatic beta-Galactosidase activity in healthy subjects and in patients affected by T2DM

Oncotarget ◽  
2017 ◽  
Vol 8 (55) ◽  
pp. 93338-93348 ◽  
Author(s):  
Liana Spazzafumo ◽  
Emanuela Mensà ◽  
Giulia Matacchione ◽  
Tiziana Galeazzi ◽  
Lucia Zampini ◽  
...  
Keyword(s):  
Healthy Subjects ◽  
Galactosidase Activity ◽  
Age Related ◽  
Beta Galactosidase

scholarly journals Age-related changes in the physical properties, cross-linking, and glycation of collagen from mouse tail tendon

2020 ◽  
Vol 295 (31) ◽  
pp. 10562-10571 ◽  
Author(s):  
Melanie Stammers ◽  
Irina M. Ivanova ◽  
Izabella S. Niewczas ◽  
Anne Segonds-Pichon ◽  
Matthew Streeter ◽  
...  
Keyword(s):  
The Other ◽  
Cross Linking ◽  
Structural Protein ◽  
Cross Link ◽  
Age Related ◽  
Cross Links ◽  
Tail Tendon ◽  
Collagen Cross Linking ◽  
Age Related Changes ◽  
Tendon Collagen

Collagen is a structural protein whose internal cross-linking critically determines the properties and functions of connective tissue. Knowing how the cross-linking of collagen changes with age is key to understanding why the mechanical properties of tissues change over a lifetime. The current scientific consensus is that collagen cross-linking increases with age and that this increase leads to tendon stiffening. Here, we show that this view should be reconsidered. Using MS-based analyses, we demonstrated that during aging of healthy C57BL/6 mice, the overall levels of collagen cross-linking in tail tendon decreased with age. However, the levels of lysine glycation in collagen, which is not considered a cross-link, increased dramatically with age. We found that in 16-week-old diabetic db/db mice, glycation reaches levels similar to those observed in 98-week-old C57BL/6 mice, while the other cross-links typical of tendon collagen either decreased or remained the same as those observed in 20-week-old WT mice. These results, combined with findings from mechanical testing of tendons from these mice, indicate that overall collagen cross-linking in mouse tendon decreases with age. Our findings also reveal that lysine glycation appears to be an important factor that contributes to tendon stiffening with age and in diabetes.

Age-Related Changes in Distribution of Body Weight on Soles of Feet for Selected Actions and Postures

1997 ◽  
Vol 85 (3_suppl) ◽  
pp. 1263-1271 ◽  
Author(s):  
Toshiaki Yanagida ◽  
Takaaki Asami
Keyword(s):  
Body Weight ◽  
Weight Distribution ◽  
Healthy Subjects ◽  
Age Groups ◽  
The Body ◽  
The Other ◽  
Elderly Subjects ◽  
Age Related ◽  
Soles Of The Feet ◽  
Age Related Changes

We investigated age-related changes in the distribution of body weight on soles of feet in 878 healthy subjects ranging from 5 to 80 years of age. By modifying Morton's Staticometer, we constructed an instrument for measuring body-weight distribution over three areas of soles of the feet, the big toe (inner forefoot), the other four toes combined (outer forefoot) and the heels for both feet, thus a total of six areas. The weights in the six areas were recorded at the completion of nine selected actions and postures. We observed that for inhaling and exhaling standing postures, generally younger subjects had a ratio close to 1:2:3 for weights recorded for the inner toe:outer toes:heels as observed by Morton, but elderly subjects had a smaller value than 3 for the heel. The body-weight distribution tended to shift from heels to outer toes across age groups, which was more distinctly observed in women than in men.

scholarly journals Immunoelectrophoretic studies on human small-intestinal brush-border proteins

1981 ◽  
Vol 193 (3) ◽  
pp. 887-890 ◽  
Author(s):  
H Skovbjerg
Keyword(s):  
Enzyme Activity ◽  
Brush Border ◽  
Dipeptidyl Peptidase ◽  
Enzyme Synthesis ◽  
Dipeptidyl Peptidase Iv ◽  
Immunoreactive Protein ◽  
Intestinal Brush Border ◽  
Small Intestinal ◽  
Brush Border Enzyme

The amounts of lactase (beta-D-galactosidase, EC 3.2.1.23), sucrase (sucrose alpha-D-glucohydrolase, EC 3.2.1.48), maltase (alpha-D-glucosidase, EC 3.2.1.20) microvillus aminopeptidase (EC 3.4.11.2) and dipeptidyl peptidase IV (EC 3.4.14.-) in tangentially sectioned biopsies from jejunum were studied by quantitative immunoelectrophoresis and enzymic assays. All enzymes had their maximum activities near the mid-region of the villi and their lowest activities at the bases of the crypts. The ratio between enzyme activity and immunoreactive protein was constant along the villus-crypt axis. This result is consistent with a continuous brush-border-enzyme synthesis as the enterocytes migrate up the villi.

Age-related changes in brush border enzymes under different dietary conditions

1989 ◽  
Vol 47 (1) ◽  
pp. 55-64 ◽  
Author(s):  
Masatoshi Nakano ◽  
Hisashi Tauchi ◽  
Haruko Katoh ◽  
Hironobu Kondoh
Keyword(s):  
Brush Border ◽  
Brush Border Enzymes ◽  
Age Related ◽  
Age Related Changes

scholarly journals Human small-intestinal β-galactosidases. Separation and characterization of one lactase and one hetero β-galactosidase

1969 ◽  
Vol 114 (2) ◽  
pp. 351-359 ◽  
Author(s):  
Nils-Georg Asp ◽  
Arne Dahlqvist ◽  
Otakar Koldovský
Keyword(s):  
Intestinal Mucosa ◽  
Gel Filtration ◽  
Competitive Inhibitor ◽  
The Other ◽  
Artificial Substrates ◽  
Small Intestinal Mucosa ◽  
Lactase Activity ◽  
Ph Optimum ◽  
Small Intestinal

1. Two β-galactosidases from human small-intestinal mucosa were separated by gel-filtration chromatography and the properties of the two enzymes were studied. Lactose and four hetero β-galactosides were used as substrates. 2. One of the enzymes was particle-bound and could be partially solubilized with papain. Of the substrates hydrolysed by this enzyme, lactose was hydrolysed most rapidly. This enzyme is thus essentially a disaccharidase and is named lactase. It is presumably identical with the ‘lactase 1’ described earlier. 3. The other enzyme was mainly soluble and hydrolysed all artificial substrates used, whereas no lactase activity could be detected. This enzyme has therefore been designated hetero β-galactosidase. 4. p-Chloromercuribenzoate (0·1mm) inhibited the hetero β-galactosidase completely but did not influence the activity of the lactase. Tris was a competitive inhibitor of both enzymes. 5. The residual lactase activity in the mucosa of lactose-intolerant patients may be exerted by a small amount of remaining lactase as such, or possibly by a third enzyme with a more acid pH optimum.

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