Further characterization of intestinal lactase/phlorizin hydrolase

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Standard

Further characterization of intestinal lactase/phlorizin hydrolase. / Skovbjerg, H; Norén, O; Sjöström, H; Danielsen, Erik Michael; Enevoldsen, B S.

I: BBA General Subjects, Bind 707, Nr. 1, 1982, s. 89-97.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Skovbjerg, H, Norén, O, Sjöström, H, Danielsen, EM & Enevoldsen, BS 1982, 'Further characterization of intestinal lactase/phlorizin hydrolase', BBA General Subjects, bind 707, nr. 1, s. 89-97.

APA

Skovbjerg, H., Norén, O., Sjöström, H., Danielsen, E. M., & Enevoldsen, B. S. (1982). Further characterization of intestinal lactase/phlorizin hydrolase. BBA General Subjects, 707(1), 89-97.

Vancouver

Skovbjerg H, Norén O, Sjöström H, Danielsen EM, Enevoldsen BS. Further characterization of intestinal lactase/phlorizin hydrolase. BBA General Subjects. 1982;707(1):89-97.

Author

Skovbjerg, H ; Norén, O ; Sjöström, H ; Danielsen, Erik Michael ; Enevoldsen, B S. / Further characterization of intestinal lactase/phlorizin hydrolase. I: BBA General Subjects. 1982 ; Bind 707, Nr. 1. s. 89-97.

Bibtex

@article{f74c82906c7a11de8bc9000ea68e967b,
title = "Further characterization of intestinal lactase/phlorizin hydrolase",
abstract = "Pig intestinal lactase/phlorizin hydrolase (EC 3.2.1.23/62) was purified in its amphiphilic form by immunoadsorbent chromatography. The purified enzyme was free of other known brush border enzymes and appeared homogeneous in immunoelectrophoresis and polyacrylamide gel electrophoresis in the presence of SDS. Pig lactase/phlorizin hydrolase was shown to have the same quaternary structure as the human enzyme, i.e., built up of two polypeptides of the same molecular weight (160000). In addition to hydrolyzing lactose, phlorizin and a number of synthetic substrates, both the human and the pig enzyme were shown to have a considerable activity against cellotriose and cellotetraose, and a low but significant activity against cellulose. The lactase/phlorizin hydrolase isolated from pigs in which the pancreatic ducts had been disconnected 3 days before death and from Ca2+-precipitated enterocyte membranes (basolateral and intracellular membranes) exhibited in SDS-polyacrylamide gel electrophoresis the same size of constituent polypeptides and the same catalytic and immunological properties as a normal brush border lactase/phlorizin hydrolase.",
author = "H Skovbjerg and O Nor{\'e}n and H Sj{\"o}str{\"o}m and Danielsen, {Erik Michael} and Enevoldsen, {B S}",
note = "Keywords: Animals; Galactosidases; Glucosidases; Glycosylceramidase; Humans; Immunoelectrophoresis, Two-Dimensional; Intestine, Small; Kinetics; Microvilli; Molecular Weight; Species Specificity; Substrate Specificity; Swine; beta-Galactosidase",
year = "1982",
language = "English",
volume = "707",
pages = "89--97",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "1",

}

RIS

TY - JOUR

T1 - Further characterization of intestinal lactase/phlorizin hydrolase

AU - Skovbjerg, H

AU - Norén, O

AU - Sjöström, H

AU - Danielsen, Erik Michael

AU - Enevoldsen, B S

N1 - Keywords: Animals; Galactosidases; Glucosidases; Glycosylceramidase; Humans; Immunoelectrophoresis, Two-Dimensional; Intestine, Small; Kinetics; Microvilli; Molecular Weight; Species Specificity; Substrate Specificity; Swine; beta-Galactosidase

PY - 1982

Y1 - 1982

N2 - Pig intestinal lactase/phlorizin hydrolase (EC 3.2.1.23/62) was purified in its amphiphilic form by immunoadsorbent chromatography. The purified enzyme was free of other known brush border enzymes and appeared homogeneous in immunoelectrophoresis and polyacrylamide gel electrophoresis in the presence of SDS. Pig lactase/phlorizin hydrolase was shown to have the same quaternary structure as the human enzyme, i.e., built up of two polypeptides of the same molecular weight (160000). In addition to hydrolyzing lactose, phlorizin and a number of synthetic substrates, both the human and the pig enzyme were shown to have a considerable activity against cellotriose and cellotetraose, and a low but significant activity against cellulose. The lactase/phlorizin hydrolase isolated from pigs in which the pancreatic ducts had been disconnected 3 days before death and from Ca2+-precipitated enterocyte membranes (basolateral and intracellular membranes) exhibited in SDS-polyacrylamide gel electrophoresis the same size of constituent polypeptides and the same catalytic and immunological properties as a normal brush border lactase/phlorizin hydrolase.

AB - Pig intestinal lactase/phlorizin hydrolase (EC 3.2.1.23/62) was purified in its amphiphilic form by immunoadsorbent chromatography. The purified enzyme was free of other known brush border enzymes and appeared homogeneous in immunoelectrophoresis and polyacrylamide gel electrophoresis in the presence of SDS. Pig lactase/phlorizin hydrolase was shown to have the same quaternary structure as the human enzyme, i.e., built up of two polypeptides of the same molecular weight (160000). In addition to hydrolyzing lactose, phlorizin and a number of synthetic substrates, both the human and the pig enzyme were shown to have a considerable activity against cellotriose and cellotetraose, and a low but significant activity against cellulose. The lactase/phlorizin hydrolase isolated from pigs in which the pancreatic ducts had been disconnected 3 days before death and from Ca2+-precipitated enterocyte membranes (basolateral and intracellular membranes) exhibited in SDS-polyacrylamide gel electrophoresis the same size of constituent polypeptides and the same catalytic and immunological properties as a normal brush border lactase/phlorizin hydrolase.

M3 - Journal article

C2 - 6814489

VL - 707

SP - 89

EP - 97

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 1

ER -

ID: 13063661