Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Particles of meconium sedimenting at 105,000 g contain sucrase and various brush border peptidase activities. Oligoaminopeptidase, dipeptidylaminopeptidase, and sucrase solubilized by papain from meconium particles of preterm newborns or from brush border of human fetuses during the 4th month of gestation were compared with the same enzymes prepared from adult jejunal and ileal brush border. The following are characteristics of fetal intestinal brush border enzymes: (a) a faster anodal electrophoretic mobility in polyacrylamide and in agar gel; (b) the same specific activity, as measured by quantitative crossed immunoelectrophoresis utilizing an antiserum against adult brush border membranes; (c) complete fusion of the immunoprecipitation lines with the adult enzymes by using the same antiserum; and (d) a different binding pattern to Helix pomatia lectin and lentil lectin. The results suggest that the charge difference between adult and fetal human brush border enzymes, which causes the difference in the gel electrophoretic mobility, is most probably due, at least in part, to differences in carbohydrate composition of these glycoproteins. Extensive neuraminidase digestion causes no or only minor changes of the electrophoretic mobility of the meconial enzymes. The difference between adult and meconial enzymes is therefore apparently not, or not only, due to different sialic acid content. These results suggest that many intestinal brush border enzymes in fetal life and at birth are in forms structurally different from those in adult life.
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PMID:Fetal forms of oligoaminopeptidase, dipeptidylaminopeptidase IV, and sucrase in human intestine and meconium. 636 65

The activities of various glycosidases in homogenates of the small intestinal mucosa of two adult and 18 suckling tammar wallabies (M. eugenii) aged from 6 to 50 weeks were investigated. Lactase (beta-D-galactosidase), beta-N-acetylglucosaminidase, alpha-L-fucosidase and neuraminidase activities were high during the first 34 weeks post partum and then declined to very low levels. Maltase, isomaltase, sucrase and trehalase activities were very low or absent during the first 34 weeks, and then increased. The lactase activity was unusual in being greater in the distal than the middle or proximal thirds of the intestine, and in its low pH optimum (pH 4.6), inhibition by p-chloromercuribenzene sulfonate but not by Tris, and lack of cellobiase activity. These properties are those of a lysosomal acid beta-galactosidase rather than of a brush border neutral lactase. The maltase activity had the characteristics of a lysosomal acid alpha-glucosidase early in lactation and of a brush border neutral maltase in adult animals. The significance of these findings is discussed in relation to changes in dietary carbohydrates during weaning and to the mode of digestion of milk carbohydrates by the pouch young.
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PMID:Intestinal lactase (beta-galactosidase) and other glycosidase activities in suckling and adult tammar wallabies (Macropus eugenii). 678 21