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Gut carbohydrate digestive enzymes respond differentially to oxidative stress induced by in vivo infusion of hydrogen peroxide (H 2 O 2 ) in formula‐fed piglets
Author(s) -
Lackeyram Dale,
Archbold Tania,
Shoveller AnnaKate,
Mine Yoshinori,
Fan Ming Z
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1076-a
Subject(s) - maltase , sucrase , lactase , disaccharidase , chemistry , medicine , oxidative stress , endocrinology , carbohydrate , hydrogen peroxide , enzyme , biochemistry , biology
We examined responses of the maximal specific activity (V max ) of key carbohydrate digestive enzymes in piglets with hydrogen peroxide (H 2 O 2 )‐induced systemic oxidative stress. Liquid formula‐fed piglets at the age of d 5 were fitted with an intraperitoneal catheter and infused with either 5 mmol H 2 O 2 /kg BW (PER, n=8) or physiologic saline (CON, n=8) in six injections daily for a period of 10 d. Jejunal enzyme activity experiments for lactase, sucrase, maltase and maltase‐glucoamylase were conducted at 37°C with substrate concentrations over two‐fold of K m values. Piglets experiencing oxidative stress had lower (P<0.05) jejunal V max for lactase and maltase (estimates±SE: PER, 6.54±0.68 vs. CON, 12.65±0.69; and PER, 57.39±1.02 vs. CON, 75.6±1.04 μmol/mg protein.min). However, there were no differences (P>0.05) in V max of maltase‐glucoamylase and sucrase (estimates±SE: PER, 0.71±0.08 vs. CON, 0.70±0.07; and PER, 10.50±1.37 vs. CON, 12.40±1.55 μmol/mg protein.min). We conclude that oxidative stress reduced intestinal lactase and maltase functions without affecting maltase‐glucoamylase and sucrase activities. Supported by OMAFRA of Canada.